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Journal articles on the topic 'C-terminal loop'

Author: Grafiati

Published: 6 September 2023

Last updated: 31 July 2025

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1

MONLEÓN, Daniel, Vicent ESTEVE, Helena KOVACS, Juan J. CALVETE, and Bernardo CELDA. "Conformation and concerted dynamics of the integrin-binding site and the C-terminal region of echistatin revealed by homonuclear NMR." Biochemical Journal 387, no. 1 (2005): 57–66. http://dx.doi.org/10.1042/bj20041343.

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Echistatin is a potent antagonist of the integrins αvβ3, α5β1 and αIIbβ3. Its full inhibitory activity depends on an RGD (Arg-Gly-Asp) motif expressed at the tip of the integrin-binding loop and on its C-terminal tail. Previous NMR structures of echistatin showed a poorly defined integrin-recognition sequence and an incomplete C-terminal tail, which left the molecular basis of the functional synergy between the RGD loop and the C-terminal region unresolved. We report a high-resolution structure of echistatin and an analysis of its internal motions by off-resonance ROESY (rotating-frame Overhau

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2

Harouaka, Djamila, and Gail W. Wertz. "Mutations in the C-Terminal Loop of the Nucleocapsid Protein Affect Vesicular Stomatitis Virus RNA Replication and Transcription Differentially." Journal of Virology 83, no. 22 (2009): 11429–39. http://dx.doi.org/10.1128/jvi.00813-09.

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ABSTRACT The 2.9-Å structure of the vesicular stomatitis virus nucleocapsid (N) protein bound to RNA shows the RNA to be tightly sequestered between the two lobes of the N protein. Domain movement of the lobes of the N protein has been postulated to facilitate polymerase access to the RNA template. We investigated the roles of individual amino acid residues in the C-terminal loop, involved in long-range interactions between N protein monomers, in forming functional ribonucleoprotein (RNP) templates. The effects of specific N protein mutations on its expression, interaction with the phosphopro

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3

Burkhart, Michael D., Paul D'Agostino, Samuel C. Kayman, and Abraham Pinter. "Involvement of the C-Terminal Disulfide-Bonded Loop of Murine Leukemia Virus SU Protein in a Postbinding Step Critical for Viral Entry." Journal of Virology 79, no. 12 (2005): 7868–76. http://dx.doi.org/10.1128/jvi.79.12.7868-7876.2005.

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ABSTRACT A role for the C-terminal domain (CTD) of murine leukemia virus (MuLV) Env protein in viral fusion was indicated by the potent inhibition of MuLV-induced fusion, but not receptor binding, by two rat monoclonal antibodies (MAbs) specific for epitopes in the CTD. Although these two MAbs, 35/56 and 83A25, have very different patterns of reactivity with viral isolates, determinants of both epitopes were mapped to the last C-terminal disulfide-bonded loop of SU (loop 10), and residues in this loop responsible for the different specificities of these MAbs were identified. Both MAbs reacted

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Qiao, Renping, Florian Weissmann, Masaya Yamaguchi, et al. "Mechanism of APC/CCDC20 activation by mitotic phosphorylation." Proceedings of the National Academy of Sciences 113, no. 19 (2016): E2570—E2578. http://dx.doi.org/10.1073/pnas.1604929113.

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Chromosome segregation and mitotic exit are initiated by the 1.2-MDa ubiquitin ligase APC/C (anaphase-promoting complex/cyclosome) and its coactivator CDC20 (cell division cycle 20). To avoid chromosome missegregation, APC/CCDC20 activation is tightly controlled. CDC20 only associates with APC/C in mitosis when APC/C has become phosphorylated and is further inhibited by a mitotic checkpoint complex until all chromosomes are bioriented on the spindle. APC/C contains 14 different types of subunits, most of which are phosphorylated in mitosis on multiple sites. However, it is unknown which of the

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5

Ren, Chunguang, Satoshi Nagao, Masaru Yamanaka, et al. "Oligomerization enhancement and two domain swapping mode detection for thermostable cytochrome c552via the elongation of the major hinge loop." Molecular BioSystems 11, no. 12 (2015): 3218–21. http://dx.doi.org/10.1039/c5mb00545k.

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High-order oligomers increased whereas N-terminal domain swapping and C-terminal domain swapping were elucidated by the insertion of Gly residues at the major hinge loop of cytochrome c<sub>552</sub>.

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Bury, Loredana, Emanuela Falcinelli, Haripriya Kuchi Bhotla та ін. "A p.Arg127Gln variant in GPIbα LRR5 allosterically enhances affinity for VWF: a novel form of platelet-type VWD". Blood Advances 6, № 7 (2022): 2236–46. http://dx.doi.org/10.1182/bloodadvances.2021005463.

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Abstract Gain-of-function (GOF) variants in GP1BA cause platelet-type von Willebrand disease (PT-VWD), a rare inherited autosomal dominant bleeding disorder characterized by enhanced platelet GPIbα to von Willebrand factor (VWF) interaction, and thrombocytopenia. To date, only 6 variants causing PT-VWD have been described, 5 in the C-terminal disulfide loop of the VWF-binding domain of GPIbα and 1 in the macroglycopeptide. GOF GP1BA variants generate a high-affinity conformation of the C-terminal disulfide loop with a consequent allosteric conformational change on another region of GPIbα, the

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7

Takemoto, D. J., L. J. Takemoto, J. Hansen, and D. Morrison. "Regulation of retinal transducin by C-terminal peptides of rhodopsin." Biochemical Journal 232, no. 3 (1985): 669–72. http://dx.doi.org/10.1042/bj2320669.

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Transducin is a multi-subunit guanine-nucleotide-binding protein that mediates signal coupling between rhodopsin and cyclic GMP phosphodiesterase in retinal rod outer segments. Whereas the T alpha subunit of transducin binds guanine nucleotides and is the activator of the phosphodiesterase, the T beta gamma subunit may function to link physically T alpha with photolysed rhodopsin. In order to determine the binding sites of rhodopsin to transducin, we have synthesized eight peptides (Rhod-1 etc.) that correspond to the C-terminal regions of rhodopsin and to several external and one internal loo

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Goch, G., H. Kozłowska, A. Wójtowicz, and A. Bierzyński. "A comparative CD and fluorescence study of a series of model calcium-binding peptides." Acta Biochimica Polonica 46, no. 3 (1999): 673–77. http://dx.doi.org/10.18388/abp.1999_4139.

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Lanthanide-saturated peptides analogous to calcium-binding loops of EF-hand proteins can be used to stabilize the alpha-helical structure of peptide or protein segments attached to their C-termini. To study conformational properties of such loop-containing hybrids it is necessary to produce them in bacteria. In peptides obtained in this way the helix will be destabilized by the negatively charged C-terminal alpha-carboxyl groups. We propose to block them by the homoserine lactone. The results presented in this paper indicate that the presence of the lactone even at the C-terminus of the loop d

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9

Blodgett, David M., Julie K. De Zutter, Kara B. Levine, Pusha Karim, and Anthony Carruthers. "Structural Basis of GLUT1 Inhibition by Cytoplasmic ATP." Journal of General Physiology 130, no. 2 (2007): 157–68. http://dx.doi.org/10.1085/jgp.200709818.

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Cytoplasmic ATP inhibits human erythrocyte glucose transport protein (GLUT1)–mediated glucose transport in human red blood cells by reducing net glucose transport but not exchange glucose transport (Cloherty, E.K., D.L. Diamond, K.S. Heard, and A. Carruthers. 1996. Biochemistry. 35:13231–13239). We investigated the mechanism of ATP regulation of GLUT1 by identifying GLUT1 domains that undergo significant conformational change upon GLUT1–ATP interaction. ATP (but not GTP) protects GLUT1 against tryptic digestion. Immunoblot analysis indicates that ATP protection extends across multiple GLUT1 do

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Wang, Zhaoxiang, Kangkang Chen, Song Liu, Jianghua Li, and Guocheng Du. "Engineering the C-Terminal Region to Enhance the Thermal Stability of Streptomyces hygroscopicus Transglutaminase." Catalysts 14, no. 10 (2024): 706. http://dx.doi.org/10.3390/catal14100706.

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To enhance the applied value of transglutaminase (TGase), various methods have been employed to improve its catalytic properties. However, most modifications have targeted the N-terminus, while the role of the C-terminus in determining TGase properties has been overlooked. In this study, we focused on enhancing the thermal stability of Streptomyces hygroscopicus TGase by engineering its C-terminal region. Modeling revealed that the C-terminal loop interacts with the N-terminal loop through hydrogen bonds between Trp331 and N-terminal residues (Asp19, Ala20, Tyr21). Removing the last C-terminal

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Darling, Sarah, Kazuyuki Fujimitsu, Kim Hou Chia, Juan Zou, Juri Rappsilber, and Hiroyuki Yamano. "The C-terminal disordered loop domain of Apc8 unlocks APC/C mitotic activation." Cell Reports 43, no. 6 (2024): 114262. http://dx.doi.org/10.1016/j.celrep.2024.114262.

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Bannister, Roger A., Symeon Papadopoulos, Claudia S. Haarmann та Kurt G. Beam. "Effects of inserting fluorescent proteins into the α1S II–III loop: insights into excitation–contraction coupling". Journal of General Physiology 134, № 1 (2009): 35–51. http://dx.doi.org/10.1085/jgp.200910241.

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In skeletal muscle, intermolecular communication between the 1,4-dihydropyridine receptor (DHPR) and RYR1 is bidirectional: orthograde coupling (skeletal excitation–contraction coupling) is observed as depolarization-induced Ca2+ release via RYR1, and retrograde coupling is manifested by increased L-type Ca2+ current via DHPR. A critical domain (residues 720–765) of the DHPR α1S II–III loop plays an important but poorly understood role in bidirectional coupling with RYR1. In this study, we examine the consequences of fluorescent protein insertion into different positions within the α1S II–III

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Shen, Yang, Jing-fei Dong, Gabriel M. Romo та ін. "Functional analysis of the C-terminal flanking sequence of platelet glycoprotein Ibα using canine–human chimeras". Blood 99, № 1 (2002): 145–50. http://dx.doi.org/10.1182/blood.v99.1.145.

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Platelet glycoprotein Ib-IX-V (GPIb-IX-V) mediates adhesion to von Willebrand factor (vWF) in (patho)physiological thrombus formation. vWF binds the N-terminal 282 residues of GPIbα, consisting of an N-terminal flank (His1–Ile35), 7 leucine-rich repeats (Leu36–Ala200), a C-terminal flank (Phe201–Gly268), and a sulfated tyrosine sequence (Asp269–Glu282). By expressing canine–human chimeras of GPIbα on Chinese hamster ovary cells, binding sites for functional anti-GPIbα antibodies to individual domains were previously mapped, and it was shown that leucine-rich repeats 2 to 4 were required for op

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Senda, Toshiya, Miki Senda, Takeru Hayashi, and Masanori Hatakeyama. "Structure and function of the CagA oncoprotein from Helicobacter pylori." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C839. http://dx.doi.org/10.1107/s2053273314091608.

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CagA is known as a major bacterial virulence determinant from Helicobacter pylori and is critical for gastric cancer. Upon delivery into the gastric epithelial cells, CagA localizes to the inner leaflet of the plasma membrane and promiscuously interacts with host proteins such as PAR1b and SHP2. The CagA-PAR1-SHP2 complex potentiates oncogenic signaling. Biochemical and physicochemical analyses revealed that CagA is comprises a structured N-terminal region (residues 1-876) and an intrinsically disordered C-terminal region (residues 877-1186). To understand the structure and function relationsh

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15

Mason, A. B., S. A. Brown, and W. R. Church. "A highly conserved surface loop in the C-terminal domain of ovotransferrin (residues 570-584) is remote from the receptor-binding site." Biochemical Journal 266, no. 2 (1990): 393–98. http://dx.doi.org/10.1042/bj2660393.

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A peptide corresponding to a surface loop in the C-terminal domain of chicken ovotransferrin (residues 570-584) was made by solid-phase synthesis and used to immunize rabbits. A 15-amino acid-residue disulphide-linked loop occurs in both domains of all five transferrins for which the sequence is available and lies on the opposite side of the iron-binding site from the interdomain cleft. Polyclonal antibodies to the peptide were specific for non-reduced holo-ovotransferrin and the C-terminal domain, as shown by e.l.i.s.a. and immunoblotting. The antibody did not inhibit binding of ovotransferri

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16

TOMOO, Koji, Xu SHEN, Koumei OKABE, et al. "Crystal structures of 7-methylguanosine 5′-triphosphate (m7GTP)- and P1-7-methylguanosine-P3-adenosine-5′,5′-triphosphate (m7GpppA)-bound human full-length eukaryotic initiation factor 4E: biological importance of the C-terminal flexible region." Biochemical Journal 362, no. 3 (2002): 539–44. http://dx.doi.org/10.1042/bj3620539.

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The crystal structures of the full-length human eukaryotic initiation factor (eIF) 4E complexed with two mRNA cap analogues [7-methylguanosine 5′-triphosphate (m7GTP) and P1-7-methylguanosine-P3-adenosine-5′,5′-triphosphate (m7GpppA)] were determined at 2.0Å resolution (where 1Å = 0.1nm). The flexibility of the C-terminal loop region of eIF4E complexed with m7GTP was significantly reduced when complexed with m7GpppA, suggesting the importance of the second nucleotide in the mRNA cap structure for the biological function of eIF4E, especially the fixation and orientation of the C-terminal loop r

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J. S. Loureiro, Rui, Diogo Vila-Viçosa, Miguel Machuqueiro, Eugene I. Shakhnovich та Patrícia F. N. Faísca. "The Early Phase of β2m Aggregation: An Integrative Computational Study Framed on the D76N Mutant and the ΔN6 Variant". Biomolecules 9, № 8 (2019): 366. http://dx.doi.org/10.3390/biom9080366.

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Human β2-microglobulin (b2m) protein is classically associated with dialysis-related amyloidosis (DRA). Recently, the single point mutant D76N was identified as the causative agent of a hereditary systemic amyloidosis affecting visceral organs. To get insight into the early stage of the β2m aggregation mechanism, we used molecular simulations to perform an in depth comparative analysis of the dimerization phase of the D76N mutant and the ΔN6 variant, a cleaved form lacking the first six N-terminal residues, which is a major component of ex vivo amyloid plaques from DRA patients. We also provid

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18

Sugishima, Masakazu, Kei Wada, Keiichi Fukuyama та Ken Yamamoto. "Crystal structure of phytochromobilin synthase in complex with biliverdin IXα, a key enzyme in the biosynthesis of phytochrome". Journal of Biological Chemistry 295, № 3 (2019): 771–82. http://dx.doi.org/10.1074/jbc.ra119.011431.

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Phytochromobilin (PΦB) is a red/far-red light sensory pigment in plant phytochrome. PΦB synthase is a ferredoxin-dependent bilin reductase (FDBR) that catalyzes the site-specific reduction of bilins, which are sensory and photosynthesis pigments, and produces PΦB from biliverdin, a heme-derived linear tetrapyrrole pigment. Here, we determined the crystal structure of tomato PΦB synthase in complex with biliverdin at 1.95 Å resolution. The overall structure of tomato PΦB synthase was similar to those of other FDBRs, except for the addition of a long C-terminal loop and short helices. The struct

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19

Cherry, Amy L., Caitriona A. Dennis, Andrew Baron, Leslie E. Eisele, Pia A. Thommes, and Joachim Jaeger. "Hydrophobic and Charged Residues in the C-Terminal Arm of Hepatitis C Virus RNA-Dependent RNA Polymerase Regulate Initiation and Elongation." Journal of Virology 89, no. 4 (2014): 2052–63. http://dx.doi.org/10.1128/jvi.01106-14.

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ABSTRACTThe RNA-dependent RNA polymerase (RdRp) of hepatitis C virus (HCV) is essential for viral genome replication. Crystal structures of the HCV RdRp reveal two C-terminal features, a β-loop and a C-terminal arm, suitably located for involvement in positioning components of the initiation complex. Here we show that these two elements intimately regulate template and nucleotide binding, initiation, and elongation. We constructed a series of β-loop and C-terminal arm mutants, which were used forin vitroanalysis of RdRpde novoinitiation and primer extension activities. All mutants showed a sub

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Uesugi, Y., J. Arima, M. Iwabuchi, and T. Hatanaka. "C-terminal loop of Streptomyces phospholipase D has multiple functional roles." Protein Science 16, no. 2 (2006): 197–207. http://dx.doi.org/10.1110/ps.062537907.

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21

Yano, Yoshiaki, Takuya Shimbo, Yukihiko Sugimoto та Katsumi Matsuzaki. "Intracellular third loop–C-terminal tail interaction in prostaglandin EP3β receptor". Biochemical and Biophysical Research Communications 371, № 4 (2008): 846–49. http://dx.doi.org/10.1016/j.bbrc.2008.04.180.

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Strzelecka-Gołaszewska, H., M. Mossakowska, A. Woźniak, J. Moraczewska, and H. Nakayama. "Long-range conformational effects of proteolytic removal of the last three residues of actin." Biochemical Journal 307, no. 2 (1995): 527–34. http://dx.doi.org/10.1042/bj3070527.

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Truncated derivatives of actin devoid of either the last two (actin-2C) or three residues (actin-3C) were used to study the role of the C-terminal segment in the polymerization of actin. The monomer critical concentration and polymerization rate increased in the order: intact actin < actin-2C < actin-3C. Conversely, the rate of hydrolysis of actin-bound ATP during spontaneous polymerization of Mg-actin decreased in the same order, so that, for actin-3C, the ATP hydrolysis significantly lagged behind the polymer growth. Probing the conformation of the nucleotide site in the monomer form b

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23

Koschel, Matthias, Reiner Thomssen, and Volker Bruss. "Extensive Mutagenesis of the Hepatitis B Virus Core Gene and Mapping of Mutations That Allow Capsid Formation." Journal of Virology 73, no. 3 (1999): 2153–60. http://dx.doi.org/10.1128/jvi.73.3.2153-2160.1999.

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ABSTRACT We generated a large number of mutations in the hepatitis B virus (HBV) core gene inserted into a bacterial expression vector. The new mutagenesis procedure generated deletions and insertions (as sequence repeats) of various lengths at random positions between M1 and E145 but not substitutions. The R-rich 30-amino-acid C-terminal domain was not analyzed. A total of 50,000 colonies were tested with a polyclonal human serum for the expression of hepatitis B core or e antigen. A total of 110 mutants randomly chosen from 1,500 positive colonies were genotyped. Deletions and insertions wer

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Gul, Mehreen, Ahmad Navid, Muhammad Fakhar, and Sajid Rashid. "SHP-1 tyrosine phosphatase binding to c-Src kinase phosphor-dependent conformations: A comparative structural framework." PLOS ONE 18, no. 1 (2023): e0278448. http://dx.doi.org/10.1371/journal.pone.0278448.

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SHP-1 is a cytosolic tyrosine phosphatase that is primarily expressed in hematopoietic cells. It acts as a negative regulator of numerous signaling pathways and controls multiple cellular functions involved in cancer pathogenesis. This study describes the binding preferences of SHP-1 (pY536) to c-Srcopen (pY416) and c-Srcclose (pY527) through in silico approaches. Molecular dynamics simulation analysis revealed more conformational changes in c-Srcclose upon binding to SHP-1, as compared to its active/open conformation that is stabilized by the cooperative binding of the C-SH2 domain and C-term

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Kouchi, Zen, and Masaki Kojima. "C1-linker region of PARG1 RhoGAP promotes the catalytic recognition fold of RhoA substrate." PLOS One 20, no. 7 (2025): e0326924. https://doi.org/10.1371/journal.pone.0326924.

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PARG1 (ArhGAP29) belongs to a class of F-BAR proteins that contain a GTPase activating (GAP) domain that stimulates the GTP-to-GDP conversion of RhoGTPases. In this study, the substrate-recognition mechanism of human PARG1 was structurally modeled in computational approaches. Docking analysis using HDOCK showed that the predicted RhoGAP domain containing the N-terminal C1 region harbored structural determinants only for RhoA recognition with its catalytic loop and the α4- and α9–10 helices of the GAP domain. Molecular dynamics of wild-type PARG1-RhoA complex revealed that the predicted C1 stru

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Sierra-Valdez, Francisco, Caleigh M. Azumaya, Luis O. Romero, Terunaga Nakagawa, and Julio F. Cordero-Morales. "Structure–function analyses of the ion channel TRPC3 reveal that its cytoplasmic domain allosterically modulates channel gating." Journal of Biological Chemistry 293, no. 41 (2018): 16102–14. http://dx.doi.org/10.1074/jbc.ra118.005066.

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The transient receptor potential ion channels support Ca2+ permeation in many organs, including the heart, brain, and kidney. Genetic mutations in transient receptor potential cation channel subfamily C member 3 (TRPC3) are associated with neurodegenerative diseases, memory loss, and hypertension. To better understand the conformational changes that regulate TRPC3 function, we solved the cryo-EM structures for the full-length human TRPC3 and its cytoplasmic domain (CPD) in the apo state at 5.8- and 4.0-Å resolution, respectively. These structures revealed that the TRPC3 transmembrane domain re

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Vranken, Wim F., Miloš Buděšínský, Franky Fant, Kris Boulez, Hélène Gras-Masse, and Frans A. M. Borremans. "Conformational Features of a Synthetic Cyclic Peptide Corresponding to the Complete V3 Loop of the ELI HIV-1 Strain in Water." Collection of Czechoslovak Chemical Communications 61, no. 5 (1996): 742–50. http://dx.doi.org/10.1135/cccc19960742.

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The disulfide bridge closed cyclic peptide corresponding to the whole V3 loop of the envelope protein gp120 of the ELI HIV-1 strain was synthesized and examined by proton 2D NMR spectroscopy in water. Although the peptide is mainly conformationally flexible, a turn appears to be present at an N-terminal glycosylation site, while in the C-terminal half of the peptide the data point toward nascent helical structures. Similar conformational preferences in aqueous solution were observed in other V3 loop peptides, especially for the Ile28-Gly30 tripeptide part.

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Ostapenko, Denis, and Mark J. Solomon. "Phosphorylation by Cak1 Regulates the C-Terminal Domain Kinase Ctk1 in Saccharomyces cerevisiae." Molecular and Cellular Biology 25, no. 10 (2005): 3906–13. http://dx.doi.org/10.1128/mcb.25.10.3906-3913.2005.

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ABSTRACT Ctk1 is a Saccharomyces cerevisiae cyclin-dependent protein kinase (CDK) that assembles with Ctk2 and Ctk3 to form an active protein kinase complex, CTDK-I. CTDK-I phosphorylates Ser2 within the RNA polymerase II C-terminal domain, an activity that is required for efficient transcriptional elongation and 3′ RNA processing. Ctk1 contains a conserved T loop, which undergoes activating phosphorylation in other CDKs. We show that Ctk1 is phosphorylated on Thr-338 within the T loop. Mutation of this residue abolished Ctk1 kinase activity in vitro and resulted in a cold-sensitive phenotype.

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Langedijk, Johannes P. M. "Translocation Activity of C-terminal Domain of Pestivirus Ernsand Ribotoxin L3 Loop." Journal of Biological Chemistry 277, no. 7 (2001): 5308–14. http://dx.doi.org/10.1074/jbc.m104147200.

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Truong, Amy B., Shane C. Masters, Hongzhu Yang, and Haian Fu. "Role of the 14-3-3 C-terminal loop in ligand interaction." Proteins: Structure, Function, and Bioinformatics 49, no. 3 (2002): 321–25. http://dx.doi.org/10.1002/prot.10210.

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Lee, Haekyung, Hyukwoo Shin, Eckard Wimmer, and Aniko V. Paul. "cis-Acting RNA Signals in the NS5B C-Terminal Coding Sequence of the Hepatitis C Virus Genome." Journal of Virology 78, no. 20 (2004): 10865–77. http://dx.doi.org/10.1128/jvi.78.20.10865-10877.2004.

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ABSTRACT The cis-replicating RNA elements in the 5′ and 3′ nontranslated regions (NTRs) of the hepatitis C virus (HCV) genome have been thoroughly studied before. However, no cis-replicating elements have been identified in the coding sequences of the HCV polyprotein until very recently. The existence of highly conserved and stable stem-loop structures in the RNA polymerase NS5B coding sequence, however, has been previously predicted (A. Tuplin, J. Wood, D. J. Evans, A. H. Patel, and P. Simmonds, RNA 8:824-841, 2002). We have selected for our studies a 249-nt-long RNA segment in the C-terminal

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Chen, Yi-Chun, Yao-Tsung Chang, Chiu-Yueh Chen, et al. "Structural Insight into Integrin Recognition and Anticancer Activity of Echistatin." Toxins 12, no. 11 (2020): 709. http://dx.doi.org/10.3390/toxins12110709.

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Echistatin (Ech) is a short disintegrin with a long 42NPHKGPAT C-terminal tail. We determined the 3-D structure of Ech by X-ray crystallography. Superimposition of the structures of chains A and B showed conformational differences in their RGD loops and C-termini. The chain A structure is consistent with our NMR analysis that the GPAT residues of the C-terminus cannot be observed due to high flexibility. The hydrogen bond patterns of the RGD loop and between the RGD loop and C-terminus in Ech were the same as those of the corresponding residues in medium disintegrins. The mutant with C-termina

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Law, Ruby H. P., Trifina Sofian, Wan-Ting Kan та ін. "X-ray crystal structure of the fibrinolysis inhibitor α2-antiplasmin". Blood 111, № 4 (2008): 2049–52. http://dx.doi.org/10.1182/blood-2007-09-114215.

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The serpin α2-antiplasmin (SERPINF2) is the principal inhibitor of plasmin and inhibits fibrinolysis. Accordingly, α2-antiplasmin deficiency in humans results in uncontrolled fibrinolysis and a bleeding disorder. α2-antiplasmin is an unusual serpin, in that it contains extensive N- and C-terminal sequences flanking the serpin domain. The N-terminal sequence is crosslinked to fibrin by factor XIIIa, whereas the C-terminal region mediates the initial interaction with plasmin. To understand how this may happen, we have determined the 2.65Å X-ray crystal structure of an N-terminal truncated murine

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Peverelli, Erika, Giovanna Mantovani, Davide Calebiro, et al. "The Third Intracellular Loop of the Human Somatostatin Receptor 5 Is Crucial for Arrestin Binding and Receptor Internalization after Somatostatin Stimulation." Molecular Endocrinology 22, no. 3 (2008): 676–88. http://dx.doi.org/10.1210/me.2007-0068.

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Abstract Somatostatin (SS) is a widely distributed polypeptide that exerts inhibitory effects on hormone secretion and cell proliferation by interacting with five different receptors (SST1-SST5). β-Arrestins have been implicated in regulating SST internalization, but the structural domains mediating this effect are largely unknown. The aim of this study was to characterize the intracellular mechanisms responsible for internalization of human SST5 in the rat pituitary cell line GH3 and to identify the SST5 structural domains involved in this process. To this purpose we evaluated, by fluorescenc

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Epp, Simone F., Thilo Köhler, Patrick Plésiat, Mehri Michéa-Hamzehpour, Joachim Frey, and Jean-Claude Pechère. "C-Terminal Region of Pseudomonas aeruginosa Outer Membrane Porin OprD Modulates Susceptibility to Meropenem." Antimicrobial Agents and Chemotherapy 45, no. 6 (2001): 1780–87. http://dx.doi.org/10.1128/aac.45.6.1780-1787.2001.

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ABSTRACT We investigated the unusual susceptibility to meropenem observed for seven imipenem-resistant clinical isolates of Pseudomonas aeruginosa. These strains were genetically closely related, expressed OprD, as determined by Western blot analyses, and were resistant to imipenem (>5 μg/ml) but susceptible to meropenem (<1 μg/ml). The oprD genes from two isolates were entirely sequenced, and their deduced protein sequences showed 93% identity with that of OprD of strain PAO1. The major alteration consisted of the replacement of a stretch of 12 amino acids, located in putative external

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Wang, Fanghua, Ruixia Wei, Abdelkarim Abousalham, Wuchong Chen, Bo Yang, and Yonghua Wang. "Effect of N- and C-Terminal Amino Acids on the Interfacial Binding Properties of Phospholipase D from Vibrio parahaemolyticus." International Journal of Molecular Sciences 19, no. 8 (2018): 2447. http://dx.doi.org/10.3390/ijms19082447.

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The effects of N-terminal (1–34 amino acids) and C-terminal (434–487 amino acids) amino acid sequences on the interfacial binding properties of Phospholipase D from Vibrio parahaemolyticus (VpPLD) were characterized by using monomolecular film technology. Online tools allowed the prediction of the secondary structure of the target N- and C-terminal VpPLD sequences. Various truncated forms of VpPLD with different N- or C-terminal deletions were designed, based on their secondary structure, and their membrane binding properties were examined. The analysis of the maximum insertion pressure (MIP)

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SADLISH, Heather, Frederick M. R. WILLIAMS, and Wayne F. FLINTOFF. "Cytoplasmic domains of the reduced folate carrier are essential for trafficking, but not function." Biochemical Journal 364, no. 3 (2002): 777–86. http://dx.doi.org/10.1042/bj20011361.

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The reduced folate carrier (RFC) protein has a secondary structure consistent with the predicted 12 transmembrane (TM) domains, intracellular N- and C-termini and a large cytoplasmic loop between TM6 and TM7. In the present study, the role of the cytoplasmic domains in substrate transport and protein biogenesis were examined using an array of hamster RFC deletion mutants fused to enhanced green fluorescent protein and expressed in Chinese hamster ovary cells. The N- and C-terminal tails were removed both individually and together, or the large cytoplasmic loop was modified such that the domain

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Chan, Tung O., Jin Zhang, Brian C. Tiegs, et al. "Akt kinase C-terminal modifications control activation loop dephosphorylation and enhance insulin response." Biochemical Journal 471, no. 1 (2015): 37–51. http://dx.doi.org/10.1042/bj20150325.

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This report identifies an allosteric regulatory mechanism involving C-terminal sequences and the Akt kinase domain that serves to restrict phosphatase access to the Akt activation loop. Importantly, this interaction can be modified to increase insulin sensitivity and protect cells from ceramide-mediated insulin resistance.

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Carlberg, K., and L. Rohrschneider. "The effect of activating mutations on dimerization, tyrosine phosphorylation and internalization of the macrophage colony stimulating factor receptor." Molecular Biology of the Cell 5, no. 1 (1994): 81–95. http://dx.doi.org/10.1091/mbc.5.1.81.

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Oncogenic activation of the macrophage colony stimulating factor (M-CSF) receptor (c-Fms) requires mutation or truncation of the carboxyl terminus and specific amino acid substitutions in or near the fourth immunoglobulin (Ig)-like loop in the extracellular domain. Using a murine c-Fms system, we investigated the effect of C-terminal truncation, substitutions at amino acids 301 and 374 in the fourth Ig-like loop of the extracellular domain, or the combined mutations on individual steps in receptor activation. The mutations at amino acids 301 and 374 were necessary, but not sufficient, for rece

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Sanford, J. C., Y. Pan, and M. Wessling-Resnick. "Properties of Rab5 N-terminal domain dictate prenylation of C-terminal cysteines." Molecular Biology of the Cell 6, no. 1 (1995): 71–85. http://dx.doi.org/10.1091/mbc.6.1.71.

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Rab5 is a Ras-related GTP-binding protein that is post-translationally modified by prenylation. We report here that an N-terminal domain contained within the first 22 amino acids of Rab5 is critical for efficient geranylgeranylation of the protein's C-terminal cysteines. This domain is immediately upstream from the "phosphate binding loop" common to all GTP-binding proteins and contains a highly conserved sequence recognized among members of the Rab family, referred to here as the YXYLFK motif. A truncation mutant that lacks this domain (Rab5(23-215) fails to become prenylated. However, a chim

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Zhou, Zi-Ren, Yu-Hang Zhang, Shuai Liu, Ai-Xin Song, and Hong-Yu Hu. "Length of the active-site crossover loop defines the substrate specificity of ubiquitin C-terminal hydrolases for ubiquitin chains." Biochemical Journal 441, no. 1 (2011): 143–49. http://dx.doi.org/10.1042/bj20110699.

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UCHs [Ub (ubiquitin) C-terminal hydrolases] are a family of deubiquitinating enzymes that are often thought to only remove small C-terminal peptide tails from Ub adducts. Among the four UCHs identified to date, neither UCH-L3 nor UCH-L1 can catalyse the hydrolysis of isopeptide Ub chains, but UCH-L5 can when it is present in the PA700 complex of the proteasome. In the present paper, we report that the UCH domain of UCH-L5, different from UCH-L1 and UCH-L3, by itself can process the K48-diUb (Lys48-linked di-ubiquitin) substrate by cleaving the isopeptide bond between two Ub units. The catalyti

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Okamoto, Hisayo, Tove Hammarberg, Ying-Yi Zhang, et al. "Mutation analysis of the human 5-lipoxygenase C-terminus: Support for a stabilizing C-terminal loop." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1749, no. 1 (2005): 123–31. http://dx.doi.org/10.1016/j.bbapap.2005.03.005.

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Pearson, Adam J., Paul Fullwood, Gabriela Toro Tapia, et al. "Discovery of a Gatekeeper Residue in the C-Terminal Tail of the Extracellular Signal-Regulated Protein Kinase 5 (ERK5)." International Journal of Molecular Sciences 21, no. 3 (2020): 929. http://dx.doi.org/10.3390/ijms21030929.

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The extracellular signal-regulated protein kinase 5 (ERK5) is a non-redundant mitogen-activated protein kinase (MAPK) that exhibits a unique C-terminal extension which comprises distinct structural and functional properties. Here, we sought to elucidate the significance of phosphoacceptor sites in the C-terminal transactivation domain of ERK5. We have found that Thr732 acted as a functional gatekeeper residue controlling C-terminal-mediated nuclear translocation and transcriptional enhancement. Consistently, using a non-bias quantitative mass spectrometry approach, we demonstrated that phospho

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Maerz, Anne L., Heidi E. Drummer, Kirilee A. Wilson, and Pantelis Poumbourios. "Functional Analysis of the Disulfide-Bonded Loop/Chain Reversal Region of Human Immunodeficiency Virus Type 1 gp41 Reveals a Critical Role in gp120-gp41 Association." Journal of Virology 75, no. 14 (2001): 6635–44. http://dx.doi.org/10.1128/jvi.75.14.6635-6644.2001.

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ABSTRACT Human immunodeficiency virus type 1 (HIV-1) entry into cells is mediated by the surface-exposed envelope protein (SU) gp120, which binds to cellular CD4 and chemokine receptors, triggering the membrane fusion activity of the transmembrane (TM) protein gp41. The core of gp41 comprises an N-terminal triple-stranded coiled coil and an antiparallel C-terminal helical segment which is packed against the exterior of the coiled coil and is thought to correspond to a fusion-activated conformation. The available gp41 crystal structures lack the conserved disulfide-bonded loop region which, in

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Ishii, K., H. Hayashi, M. Todaka, et al. "Possible domains responsible for intracellular targeting and insulin-dependent translocation of glucose transporter type 4." Biochemical Journal 309, no. 3 (1995): 813–23. http://dx.doi.org/10.1042/bj3090813.

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Translocation of the type 4 glucose transporter (GLUT4) to the cell surface from an intracellular pool is the major mechanism of insulin-stimulated glucose uptake in insulin-target cells. We developed a highly sensitive and quantitative method to detect GLUT4 immunologically on the surface of intact cells, using c-myc epitope-tagged GLUT4 (GLUT4myc). We constructed c-myc epitope-tagged glucose transporter type 1 (GLUT1myc) and found that the GLUT1myc was also translocated to the cell surface of Chinese hamster ovary cells, 3T3-L1 fibroblasts and NIH 3T3 cells, in response to insulin, but the d

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Labrosse, Béatrice, Carole Treboute, Anne Brelot, and Marc Alizon. "Cooperation of the V1/V2 and V3 Domains of Human Immunodeficiency Virus Type 1 gp120 for Interaction with the CXCR4 Receptor." Journal of Virology 75, no. 12 (2001): 5457–64. http://dx.doi.org/10.1128/jvi.75.12.5457-5464.2001.

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ABSTRACT Human immunodeficiency virus type 1 (HIV-1) entry is triggered by the interaction of the gp120 envelope glycoprotein with a cellular chemokine receptor, either CCR5 or CXCR4. We have identified different mutations in human CXCR4 that prevent efficient infection by one HIV-1 strain (NDK) but not another (LAI) and sought to define these strain-dependent effects at the gp120 level. The lack of activity toward the NDK strain of the HHRH chimeric CXCR4 in which the second extracellular loop (ECL2) derived from the rat CXCR4 and of CXCR4 with mutations at an aspartic acid in ECL2 (D193A and

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Rubenstein, Eric M., Rhonda R. McCartney, and Martin C. Schmidt. "Regulatory Domains of Snf1-Activating Kinases Determine Pathway Specificity." Eukaryotic Cell 5, no. 4 (2006): 620–27. http://dx.doi.org/10.1128/ec.5.4.620-627.2006.

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ABSTRACT In Saccharomyces cerevisiae, the Snf1 kinase can be activated by any one of three upstream kinases, Sak1, Tos3, or Elm1. All three Snf1-activating kinases contain serine/threonine kinase domains near their N termini and large C-terminal domains with little sequence conservation and previously unknown function. Deletion of the C-terminal domains of Sak1 and Tos3 greatly reduces their ability to activate the Snf1 pathway. In contrast, deletion of the Elm1 C-terminal domain has no effect on Snf1 signaling but abrogates the ability of Elm1 to participate in the morphogenetic-checkpoint si

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Barski, Oleg A., Kenneth H. Gabbay, and Kurt M. Bohren. "The C-Terminal Loop of Aldehyde Reductase Determines the Substrate and Inhibitor Specificity†." Biochemistry 35, no. 45 (1996): 14276–80. http://dx.doi.org/10.1021/bi9619740.

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Gómez-Moutón, Concepción, Thierry Fischer, Rosa M. Peregil, et al. "Filamin A interaction with the CXCR4 third intracellular loop regulates endocytosis and signaling of WT and WHIM-like receptors." Blood 125, no. 7 (2015): 1116–25. http://dx.doi.org/10.1182/blood-2014-09-601807.

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Key Points Filamin A interacts directly with the third intracellular loop and the C-terminal tail of CXCR4. Disruption of FLNA binding to the ICL3 attenuates signaling and restores CXCL12-mediated endocytosis of WHIM-like CXCR4 receptor mutants.

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Baruah, Avanti, Brett Lindsey, Yi Zhu, and Michiko M. Nakano. "Mutational Analysis of the Signal-Sensing Domain of ResE Histidine Kinase from Bacillus subtilis." Journal of Bacteriology 186, no. 6 (2004): 1694–704. http://dx.doi.org/10.1128/jb.186.6.1694-1704.2004.

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ABSTRACT The Bacillus subtilis ResD-ResE two-component regulatory system activates genes involved in nitrate respiration in response to oxygen limitation or nitric oxide (NO). The sensor kinase ResE activates the response regulator ResD through phosphorylation, which then binds to the regulatory region of genes involved in anaerobiosis to activate their transcription. ResE is composed of an N-terminal signal input domain and a C-terminal catalytic domain. The N-terminal domain contains two transmembrane subdomains and a large extracytoplasmic loop. It also has a cytoplasmic PAS subdomain betwe

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