Relevant bibliographies by topics / AtGLR3.3 ligand-binding domain structure

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'AtGLR3.3 ligand-binding domain structure'

Author: Grafiati
Published: 9 March 2023
Last updated: 31 July 2025

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'AtGLR3.3 ligand-binding domain structure.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "AtGLR3.3 ligand-binding domain structure"

1

Shih, DT, JM Edelman, AF Horwitz, GB Grunwald, and CA Buck. "Structure/function analysis of the integrin beta 1 subunit by epitope mapping." Journal of Cell Biology 122, no. 6 (1993): 1361–71. http://dx.doi.org/10.1083/jcb.122.6.1361.

Full text
Abstract:
Monoclonal antibodies (mAbs) have been produced against the chicken beta 1 subunit that affect integrin functions, including ligand binding, alpha subunit association, and regulation of ligand specificity. Epitope mapping of these antibodies was used to identify regions of the subunit involved in these functions. To accomplish this, we produced mouse/chicken chimeric beta 1 subunits and expressed them in mouse 3T3 cells. These chimeric subunits were fully functional with respect to heterodimer formation, cell surface expression, and cell adhesion. They differed in their ability to react with a
APA, Harvard, Vancouver, ISO, and other styles
2

Jensen, Maria Risager, Goran Bajic, Xianwei Zhang, et al. "Structural Basis for Simvastatin Competitive Antagonism of Complement Receptor 3." Journal of Biological Chemistry 291, no. 33 (2016): 16963–76. http://dx.doi.org/10.1074/jbc.m116.732222.

Full text
Abstract:
The complement system is an important part of the innate immune response to infection but may also cause severe complications during inflammation. Small molecule antagonists to complement receptor 3 (CR3) have been widely sought, but a structural basis for their mode of action is not available. We report here on the structure of the human CR3 ligand-binding I domain in complex with simvastatin. Simvastatin targets the metal ion-dependent adhesion site of the open, ligand-binding conformation of the CR3 I domain by direct contact with the chelated Mg2+ ion. Simvastatin antagonizes I domain bind
APA, Harvard, Vancouver, ISO, and other styles
3

Springer, Timothy A., Junichi Takagi, Barry S. Coller, Jia-Huai Wang та Tsan Xiao. "Crystal Structure of the Integrin αIIBβ3 Headpiece at 2.7–3.1 Å: Structure, Mechanisms of Activation and Ligand Binding, Inhibition by Eptifibatide, Tirofiban, and mAb 10E5, and Structure of the HPA-1 Alloantigen Epitope." Blood 104, № 11 (2004): 327. http://dx.doi.org/10.1182/blood.v104.11.327.327.

Full text
Abstract:
Abstract The αIIbβ3 headpiece (αIIb, 1–621; β3, 1–472) was expressed in CHO cells, purified, digested with chymotrypsin, mixed with either mAb 10E5 Fab (form A) or without (form B), repurified, digested with carboxypeptidase (leaving αIIb, 1–452 and β3, 1–440) and crystallized with PEG, Mg acetate, and Na cacodylate at 4°C. Cocrystallization of αIIbβ3/10E5 (A) with eptifibatide or tirofiban was with imidazole instead of cacodylate. Crystals were diffracted at APS and CHESS and analyzed by HKL2000, AMoRe, O, CNS, and CCP4 software. Crystal forms A and B contain 1 and 3 molecules/asymmetric unit
APA, Harvard, Vancouver, ISO, and other styles
4

Bell, J. K., I. Botos, P. R. Hall, et al. "The molecular structure of the Toll-like receptor 3 ligand-binding domain." Proceedings of the National Academy of Sciences 102, no. 31 (2005): 10976–80. http://dx.doi.org/10.1073/pnas.0505077102.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Kolenko, Petr, Daniel Rozbeský, Tereza Skálová, et al. "Domain swapping in structure of mNKR-P1A: unique feature with unknown function." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C249. http://dx.doi.org/10.1107/s2053273314097502.

Full text
Abstract:
Natural killer (NK) cells, large granular lymphocytes, play an important role in the innate immune response against viruses, parasites and tumour cells. NK cells use a wide repertoire of surface receptors to modulate their activity [1]. The family of NKR-P1 surface receptors of NK cells belong to proteins with C-type lectin-like (CTL) fold. The overall architecture of other known CTL receptors (e.g. members of Ly49 family, NKG2D, CD94, mouse CLRg) is conserved [2]. The mechanism of ligand binding has been revealed by the crystal structure of Nkp65 bound to its keratinocyte ligand [3]. However,
APA, Harvard, Vancouver, ISO, and other styles
6

Tamura, Tatsushiro, Jun Yamanouchi, Shigeru Fujita та Takaaki Hato. "Critical residues for ligand binding in blade 2 of the propeller domain of the integrin αIIb subunit". Thrombosis and Haemostasis 91, № 01 (2004): 111–18. http://dx.doi.org/10.1160/th03-06-0392.

Full text
Abstract:
SummaryLigand binding to integrin αIIbβ3 is a key event of thrombus formation. The propeller domain of the αIIb subunit has been implicated in ligand binding. Recently, the ligand binding site of the αV propeller was determined by crystal structure analysis. However, the structural basis of ligand recognition by the αIIb propeller remains to be determined. In this study, we conducted site-directed mutagenesis of all residues located in the loops extending above blades 2 and 4 of the αIIb propeller, which are spatially close to, but distinct from, the loops that contain the binding site for an
APA, Harvard, Vancouver, ISO, and other styles
7

Li, Chaoqun, Xiaojia Zhao, Xiaomin Zhu, Pengtao Xie, and Guangju Chen. "Structural Studies of the 3′,3′-cGAMP Riboswitch Induced by Cognate and Noncognate Ligands Using Molecular Dynamics Simulation." International Journal of Molecular Sciences 19, no. 11 (2018): 3527. http://dx.doi.org/10.3390/ijms19113527.

Full text
Abstract:
Riboswtich RNAs can control gene expression through the structural change induced by the corresponding small-molecule ligands. Molecular dynamics simulations and free energy calculations on the aptamer domain of the 3′,3′-cGAMP riboswitch in the ligand-free, cognate-bound and noncognate-bound states were performed to investigate the structural features of the 3′,3′-cGAMP riboswitch induced by the 3′,3′-cGAMP ligand and the specificity of ligand recognition. The results revealed that the aptamer of the 3′,3′-cGAMP riboswitch in the ligand-free state has a smaller binding pocket and a relatively
APA, Harvard, Vancouver, ISO, and other styles
8

Rossjohn, Jamie, William J. McKinstry, Joanna M. Woodcock та ін. "Structure of the activation domain of the GM-CSF/IL-3/IL-5 receptor common β-chain bound to an antagonist". Blood 95, № 8 (2000): 2491–98. http://dx.doi.org/10.1182/blood.v95.8.2491.

Full text
Abstract:
Abstract Heterodimeric cytokine receptors generally consist of a major cytokine-binding subunit and a signaling subunit. The latter can transduce signals by more than 1 cytokine, as exemplified by the granulocyte-macrophage colony-stimulating factor (GM-CSF), interleukin-2 (IL-2), and IL-6 receptor systems. However, often the signaling subunits in isolation are unable to bind cytokines, a fact that has made it more difficult to obtain structural definition of their ligand-binding sites. This report details the crystal structure of the ligand-binding domain of the GM-CSF/IL-3/IL-5 receptor β-ch
APA, Harvard, Vancouver, ISO, and other styles
9

Rossjohn, Jamie, William J. McKinstry, Joanna M. Woodcock та ін. "Structure of the activation domain of the GM-CSF/IL-3/IL-5 receptor common β-chain bound to an antagonist". Blood 95, № 8 (2000): 2491–98. http://dx.doi.org/10.1182/blood.v95.8.2491.008k06_2491_2498.

Full text
Abstract:
Heterodimeric cytokine receptors generally consist of a major cytokine-binding subunit and a signaling subunit. The latter can transduce signals by more than 1 cytokine, as exemplified by the granulocyte-macrophage colony-stimulating factor (GM-CSF), interleukin-2 (IL-2), and IL-6 receptor systems. However, often the signaling subunits in isolation are unable to bind cytokines, a fact that has made it more difficult to obtain structural definition of their ligand-binding sites. This report details the crystal structure of the ligand-binding domain of the GM-CSF/IL-3/IL-5 receptor β-chain (βc)
APA, Harvard, Vancouver, ISO, and other styles
10

Ozheriedov, D. S., and P. A. Karpov. "Structural profile of ligand-based inhibition of bacterial FtsZ." Faktori eksperimental'noi evolucii organizmiv 32 (September 1, 2023): 142–47. http://dx.doi.org/10.7124/feeo.v32.1551.

Full text
Abstract:
Aim. The idea of the study was to compare and generalize RCSB Protein Data Bank and ChEMBL data in order to establish the structural and biological relationship of experimentaly proved effectors of FtsZ with binding sites. Methods. Literature and database search. Comparison of protein and ligand structures. Protein structure modeling, MD, structural superimposition, etc. Results. The experimental protein-ligand complexes structures of bacterial FtsZ were revised. The structural superimposition of experinental PDB and full-atomic AlphaFold2 models of bacterial FtsZs confirmed their significant
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "AtGLR3.3 ligand-binding domain structure"

1

Xue, Yu Lord Susan T. "Study protein-protein interaction in methyl-directed DNA mismatch repair in E. coli exonuclease I Exo I and DNA helicas II UvrD; A minimal exonuclease domain of WRN forms a hexamer on DNA and possesses both 3'-5' exonuclease and 5'-protruding strand endonuclease activities; Solving the structure of the ligand-binding domain of the pregnane-xenobiotic-receptor with 17[beta] estradiol and T1317 /." Chapel Hill, N.C. : University of North Carolina at Chapel Hill, 2008. http://dc.lib.unc.edu/u?/etd,2015.

Full text
Abstract:
Thesis (Ph. D.)--University of North Carolina at Chapel Hill, 2008.<br>Title from electronic title page (viewed Feb. 17, 2009). "... in partial fulfillment of the requirements for the degree of Doctor of Philosophy in the Department of Chemistry." Discipline: Chemistry; Department/School: Chemistry.
APA, Harvard, Vancouver, ISO, and other styles

Book chapters on the topic "AtGLR3.3 ligand-binding domain structure"

1

Gallastegui, Nerea, and Eva Estébanez-Perpiñá. "Thinking Outside the Box: Alternative Binding Sites in the Ligand Binding Domain of Nuclear Receptors." In Nuclear Receptors: From Structure to the Clinic. Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-18729-7_10.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Reynaud, J. P., V. Bissery, C. Gaboriaud, T. Ojasoo, G. Teutsch, and J. P. Mornon. "An Analysis of the Steroid Binding Domain of Receptors and of Ligand Structure and Binding Affinity." In The Steroid/Thyroid Hormone Receptor Family and Gene Regulation. Birkhäuser Basel, 1989. http://dx.doi.org/10.1007/978-3-0348-5466-5_24.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "AtGLR3.3 ligand-binding domain structure"

1

Beeler, D., L. Fritze, G. Soff, R. Jackman, and R. Rosenberg. "HUMAN THROMBOMODULIN cDNA:SEQUENCE AND TRANSLATED STRUCTURE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643967.

Full text
Abstract:
A 750 bp bovine Thrombomodulin (TM) cDNA fragment was used as an hybridization probe to screen an oligo-dT primed Lambda gtll. cDNA library prepared from human umbilical vein endothelial cell mRNA. A 2.4 kb positive human clone was isolated which showed an 80% nucleotide sequence homology with bovine TM cDNA. This clone and a 550 bp fragment from its 5' end were used to further screen the oligo-dT primed library as well as randomly primed library prepared from the same mRNA. The cDNA clones obtained allow us to describe the overall structure of human TM and reveal that it is extremely similar
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'AtGLR3.3 ligand-binding domain structure' for particular source types:
Journal articles
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography