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Journal articles on the topic 'Class A GPCR'

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Published: 14 March 2023

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1

Vidad, Ashley Ryan, Stephen Macaspac, and Ho Leung Ng. "Locating ligand binding sites in G-protein coupled receptors using combined information from docking and sequence conservation." PeerJ 9 (September 24, 2021): e12219. http://dx.doi.org/10.7717/peerj.12219.

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GPCRs (G-protein coupled receptors) are the largest family of drug targets and share a conserved structure. Binding sites are unknown for many important GPCR ligands due to the difficulties of GPCR recombinant expression, biochemistry, and crystallography. We describe our approach, ConDockSite, for predicting ligand binding sites in class A GPCRs using combined information from surface conservation and docking, starting from crystal structures or homology models. We demonstrate the effectiveness of ConDockSite on crystallized class A GPCRs such as the beta2 adrenergic and A2A adenosine recepto

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2

Hou, Tianling, Yuemin Bian, Terence McGuire, and Xiang-Qun Xie. "Integrated Multi-Class Classification and Prediction of GPCR Allosteric Modulators by Machine Learning Intelligence." Biomolecules 11, no. 6 (2021): 870. http://dx.doi.org/10.3390/biom11060870.

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G-protein-coupled receptors (GPCRs) are the largest and most diverse group of cell surface receptors that respond to various extracellular signals. The allosteric modulation of GPCRs has emerged in recent years as a promising approach for developing target-selective therapies. Moreover, the discovery of new GPCR allosteric modulators can greatly benefit the further understanding of GPCR cell signaling mechanisms. It is critical but also challenging to make an accurate distinction of modulators for different GPCR groups in an efficient and effective manner. In this study, we focus on an 11-clas

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3

Sato. "Conserved 2nd Residue of Helix 8 of GPCR May Confer the Subclass-Characteristic and Distinct Roles through a Rapid Initial Interaction with Specific G Proteins." International Journal of Molecular Sciences 20, no. 7 (2019): 1752. http://dx.doi.org/10.3390/ijms20071752.

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To obtain a systematic view of the helix-8-second residue responsible for G protein-coupled receptor (GPCR)–G protein initial specific interactions, 786 human GPCRs were subclassified based on the pairs of agonist groups and target G proteins and compared with their conserved second residue of helix 8. Of 314 non-olfactory and deorphanized GPCRs, 273 (87%) conserved single amino acids in the subclasses, while 93 (58%) of the 160 subclasses possessed only a single GPCR member. Class B, C, Frizzled, and trace amine-associated GPCRs demonstrated 100% conservation, whereas class Ⅰ and Ⅱ olfactory

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Vohra, Shabana, Bruck Taddese, Alex C. Conner, et al. "Similarity between class A and class B G-protein-coupled receptors exemplified through calcitonin gene-related peptide receptor modelling and mutagenesis studies." Journal of The Royal Society Interface 10, no. 79 (2013): 20120846. http://dx.doi.org/10.1098/rsif.2012.0846.

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Modelling class B G-protein-coupled receptors (GPCRs) using class A GPCR structural templates is difficult due to lack of homology. The plant GPCR, GCR1, has homology to both class A and class B GPCRs. We have used this to generate a class A–class B alignment, and by incorporating maximum lagged correlation of entropy and hydrophobicity into a consensus score, we have been able to align receptor transmembrane regions. We have applied this analysis to generate active and inactive homology models of the class B calcitonin gene-related peptide (CGRP) receptor, and have supported it with site-dire

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Pellissier, Lucie P., Gaël Barthet, Florence Gaven, et al. "G Protein Activation by Serotonin Type 4 Receptor Dimers." Journal of Biological Chemistry 286, no. 12 (2011): 9985–97. http://dx.doi.org/10.1074/jbc.m110.201939.

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The discovery that class C G protein-coupled receptors (GPCRs) function as obligatory dimeric entities has generated major interest in GPCR oligomerization. Oligomerization now appears to be a common feature among all GPCR classes. However, the functional significance of this process remains unclear because, in vitro, some monomeric GPCRs, such as rhodopsin and β2-adrenergic receptors, activate G proteins. By using wild type and mutant serotonin type 4 receptors (5-HT4Rs) (including a 5-HT4-RASSL) expressed in COS-7 cells as models of class A GPCRs, we show that activation of one protomer in a

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Chattopadhyay, Amitabha. "GPCRs: Lipid-Dependent Membrane Receptors That Act as Drug Targets." Advances in Biology 2014 (October 2, 2014): 1–12. http://dx.doi.org/10.1155/2014/143023.

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G protein-coupled receptors (GPCRs) are the largest class of molecules involved in signal transduction across cell membranes and represent major targets in the development of novel drug candidates in all clinical areas. Although there have been some recent leads, structural information on GPCRs is relatively rare due to the difficulty associated with crystallization. A specific reason for this is the intrinsic flexibility displayed by GPCRs, which is necessary for their functional diversity. Since GPCRs are integral membrane proteins, interaction of membrane lipids with them constitutes an imp

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Ellisdon, Andrew M., and Michelle L. Halls. "Compartmentalization of GPCR signalling controls unique cellular responses." Biochemical Society Transactions 44, no. 2 (2016): 562–67. http://dx.doi.org/10.1042/bst20150236.

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With >800 members, G protein-coupled receptors (GPCRs) are the largest class of cell-surface signalling proteins, and their activation mediates diverse physiological processes. GPCRs are ubiquitously distributed across all cell types, involved in many diseases and are major drug targets. However, GPCR drug discovery is still characterized by very high attrition rates. New avenues for GPCR drug discovery may be provided by a recent shift away from the traditional view of signal transduction as a simple chain of events initiated from the plasma membrane. It is now apparent that GPCR signallin

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8

Guo, Yan-Zhi, Meng-Long Li, Ke-Long Wang, et al. "Fast Fourier Transform-based Support Vector Machine for Prediction of G-protein Coupled Receptor Subfamilies." Acta Biochimica et Biophysica Sinica 37, no. 11 (2005): 759–66. http://dx.doi.org/10.1111/j.1745-7270.2005.00110.x.

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Abstract Although the sequence information on G-protein coupled receptors (GPCRs) continues to grow, many GPCRs remain orphaned (i.e. ligand specificity unknown) or poorly characterized with little structural information available, so an automated and reliable method is badly needed to facilitate the identification of novel receptors. In this study, a method of fast Fourier transform-based support vector machine has been developed for predicting GPCR subfamilies according to protein's hydrophobicity. In classifying Class B, C, D and F subfamilies, the method achieved an overall Matthew's corre

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9

Fu, Zhe, Linjie Zhang, Sijin Hang, et al. "Synthesis of Coumarin Derivatives: A New Class of Coumarin-Based G Protein-Coupled Receptor Activators and Inhibitors." Polymers 14, no. 10 (2022): 2021. http://dx.doi.org/10.3390/polym14102021.

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To expand the range of daphnetin-based inhibitors/activators used for targeting G protein-coupled receptors (GPCRs) in disease treatment, twenty-five coumarin derivatives 1–25, including 7,8-dihydroxycoumarin and 7-hydroxycoumarin derivatives with various substitution patterns/groups at C3-/4- positions, were synthesized via mild Pechmann condensation and hydroxyl modification. The structures were characterized by 1H NMR, 13C NMR and ESI-MS. Their inhibition or activation activities relative to GPCRs were evaluated by double-antibody sandwich ELISA (DAS–ELISA) in vitro. The results showed that

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Wright, Shane C., Maria Consuelo Alonso Cañizal, Tobias Benkel та ін. "FZD5 is a Gαq-coupled receptor that exhibits the functional hallmarks of prototypical GPCRs". Science Signaling 11, № 559 (2018): eaar5536. http://dx.doi.org/10.1126/scisignal.aar5536.

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Frizzleds (FZDs) are a group of seven transmembrane–spanning (7TM) receptors that belong to class F of the G protein–coupled receptor (GPCR) superfamily. FZDs bind WNT proteins to stimulate diverse signaling cascades involved in embryonic development, stem cell regulation, and adult tissue homeostasis. Frizzled 5 (FZD5) is one of the most studied class F GPCRs that promote the functional inactivation of the β-catenin destruction complex in response to WNTs. However, whether FZDs function as prototypical GPCRs has been heavily debated and, in particular, FZD5 has not been shown to activate hete

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Lazim, Raudah, Donghyuk Suh, Jai Woo Lee, Thi Ngoc Lan Vu, Sanghee Yoon, and Sun Choi. "Structural Characterization of Receptor–Receptor Interactions in the Allosteric Modulation of G Protein-Coupled Receptor (GPCR) Dimers." International Journal of Molecular Sciences 22, no. 6 (2021): 3241. http://dx.doi.org/10.3390/ijms22063241.

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G protein-coupled receptor (GPCR) oligomerization, while contentious, continues to attract the attention of researchers. Numerous experimental investigations have validated the presence of GPCR dimers, and the relevance of dimerization in the effectuation of physiological functions intensifies the attractiveness of this concept as a potential therapeutic target. GPCRs, as a single entity, have been the main source of scrutiny for drug design objectives for multiple diseases such as cancer, inflammation, cardiac, and respiratory diseases. The existence of dimers broadens the research scope of G

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Kruse, Andrew C., Aashish Manglik, Brian K. Kobilka, and William I. Weis. "Applications of molecular replacement to G protein-coupled receptors." Acta Crystallographica Section D Biological Crystallography 69, no. 11 (2013): 2287–92. http://dx.doi.org/10.1107/s090744491301322x.

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G protein-coupled receptors (GPCRs) are a large class of integral membrane proteins involved in regulating virtually every aspect of human physiology. Despite their profound importance in human health and disease, structural information regarding GPCRs has been extremely limited until recently. With the advent of a variety of new biochemical and crystallographic techniques, the structural biology of GPCRs has advanced rapidly, offering key molecular insights into GPCR activation and signal transduction. To date, almost all GPCR structures have been solved using molecular-replacement techniques

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Berger, Miles, David W. Scheel, Hector Macias та ін. "Gαi/o-coupled receptor signaling restricts pancreatic β-cell expansion". Proceedings of the National Academy of Sciences 112, № 9 (2015): 2888–93. http://dx.doi.org/10.1073/pnas.1319378112.

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Gi-GPCRs, G protein-coupled receptors that signal via Gα proteins of the i/o class (Gαi/o), acutely regulate cellular behaviors widely in mammalian tissues, but their impact on the development and growth of these tissues is less clear. For example, Gi-GPCRs acutely regulate insulin release from pancreatic β cells, and variants in genes encoding several Gi-GPCRs—including the α-2a adrenergic receptor, ADRA2A—increase the risk of type 2 diabetes mellitus. However, type 2 diabetes also is associated with reduced total β-cell mass, and the role of Gi-GPCRs in establishing β-cell mass is unknown. T

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Kwon, Yong-Jun, Weontae Lee, Auguste Genovesio, and Neil Emans. "A High-Content Subtractive Screen for Selecting Small Molecules Affecting Internalization of GPCRs." Journal of Biomolecular Screening 17, no. 3 (2011): 379–85. http://dx.doi.org/10.1177/1087057111427347.

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G-protein–coupled receptors (GPCRs) are pivotal in cellular responses to the environment and are common drug targets. Identification of selective small molecules acting on single GPCRs is complicated by the shared machinery coupling signal transduction to physiology. Here, we demonstrate a high-content screen using a panel of GPCR assays to identify receptor selective molecules acting within the kinase/phosphatase inhibitor family. A collection of 88 kinase and phosphatase inhibitors was screened against seven agonist-induced GPCR internalization cell models as well as transferrin uptake in hu

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Kapolka, N. J., G. J. Taghon, J. B. Rowe, et al. "DCyFIR: a high-throughput CRISPR platform for multiplexed G protein-coupled receptor profiling and ligand discovery." Proceedings of the National Academy of Sciences 117, no. 23 (2020): 13117–26. http://dx.doi.org/10.1073/pnas.2000430117.

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More than 800 G protein-coupled receptors (GPCRs) comprise the largest class of membrane receptors in humans. While there is ample biological understanding and many approved drugs for prototypic GPCRs, most GPCRs still lack well-defined biological ligands and drugs. Here, we report our efforts to tap the potential of understudied GPCRs by developing yeast-based technologies for high-throughput clustered regularly interspaced short palindromic repeats (CRISPR) engineering and GPCR ligand discovery. We refer to these technologies collectively as Dynamic Cyan Induction by Functional Integrated Re

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Bemister-Buffington, Joseph, Alex J. Wolf, Sebastian Raschka, and Leslie A. Kuhn. "Machine Learning to Identify Flexibility Signatures of Class A GPCR Inhibition." Biomolecules 10, no. 3 (2020): 454. http://dx.doi.org/10.3390/biom10030454.

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We show that machine learning can pinpoint features distinguishing inactive from active states in proteins, in particular identifying key ligand binding site flexibility transitions in GPCRs that are triggered by biologically active ligands. Our analysis was performed on the helical segments and loops in 18 inactive and 9 active class A G protein-coupled receptors (GPCRs). These three-dimensional (3D) structures were determined in complex with ligands. However, considering the flexible versus rigid state identified by graph-theoretic ProFlex rigidity analysis for each helix and loop segment wi

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Huang, Shuya Kate, and R. Scott Prosser. "Dynamics and mechanistic underpinnings to pharmacology of class A GPCRs: an NMR perspective." American Journal of Physiology-Cell Physiology 322, no. 4 (2022): C739—C753. http://dx.doi.org/10.1152/ajpcell.00044.2022.

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One-third of current pharmaceuticals target G protein-coupled receptors (GPCRs), the largest receptor superfamily in humans and mediators of diverse physiological processes. This review summarizes the recent progress in GPCR structural dynamics, focusing on class A receptors and insights derived from nuclear magnetic resonance (NMR) and other spectroscopic techniques. We describe the structural aspects of GPCR activation and the various pharmacological models that capture aspects of receptor signaling behavior. Spectroscopic studies revealed that receptors and their signaling complexes are dyn

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18

Sakmar, Thomas P. "Clicking class B GPCR ligands." Nature Chemical Biology 7, no. 8 (2011): 500–501. http://dx.doi.org/10.1038/nchembio.621.

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19

Saikia, Surovi, Manobjyoti Bordoloi, and Rajeev Sarmah. "Established and In-trial GPCR Families in Clinical Trials: A Review for Target Selection." Current Drug Targets 20, no. 5 (2019): 522–39. http://dx.doi.org/10.2174/1389450120666181105152439.

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The largest family of drug targets in clinical trials constitute of GPCRs (G-protein coupled receptors) which accounts for about 34% of FDA (Food and Drug Administration) approved drugs acting on 108 unique GPCRs. Factors such as readily identifiable conserved motif in structures, 127 orphan GPCRs despite various de-orphaning techniques, directed functional antibodies for validation as drug targets, etc. has widened their therapeutic windows. The availability of 44 crystal structures of unique receptors, unexplored non-olfactory GPCRs (encoded by 50% of the human genome) and 205 ligand recepto

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Dijkman, Patricia M., Juan C. Muñoz-García, Steven R. Lavington, et al. "Conformational dynamics of a G protein–coupled receptor helix 8 in lipid membranes." Science Advances 6, no. 33 (2020): eaav8207. http://dx.doi.org/10.1126/sciadv.aav8207.

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G protein–coupled receptors (GPCRs) are the largest and pharmaceutically most important class of membrane proteins encoded in the human genome, characterized by a seven-transmembrane helix architecture and a C-terminal amphipathic helix 8 (H8). In a minority of GPCR structures solved to date, H8 either is absent or adopts an unusual conformation. The controversial existence of H8 of the class A GPCR neurotensin receptor 1 (NTS1) has been examined here for the nonthermostabilized receptor in a functionally supporting membrane environment using electron paramagnetic resonance, molecular dynamics

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Wheatley, Mark, Jack Charlton, Mohammed Jamshad, et al. "GPCR–styrene maleic acid lipid particles (GPCR–SMALPs): their nature and potential." Biochemical Society Transactions 44, no. 2 (2016): 619–23. http://dx.doi.org/10.1042/bst20150284.

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G-protein-coupled receptors (GPCRs) form the largest class of membrane proteins and are an important target for therapeutic drugs. These receptors are highly dynamic proteins sampling a range of conformational states in order to fulfil their complex signalling roles. In order to fully understand GPCR signalling mechanisms it is necessary to extract the receptor protein out of the plasma membrane. Historically this has universally required detergents which inadvertently strip away the annulus of lipid in close association with the receptor and disrupt lateral pressure exerted by the bilayer. De

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Akondi, Kalyana Bharati, Marianne Paolini-Bertrand, and Oliver Hartley. "Precision-engineered Peptide and Protein Analogs: Establishing a New Discovery Platform for Potent GPCR Modulators." CHIMIA International Journal for Chemistry 75, no. 6 (2021): 489–94. http://dx.doi.org/10.2533/chimia.2021.489.

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Numerous members of the human G protein-coupled receptor (GPCR) superfamily are receptors of therapeutic interest. GPCRs are considered to be highly tractable for drug discovery, representing the targets of approximately one-third of currently licensed drugs. These successful drug discovery outcomes cover only a relatively small subset of the superfamily, however, and many other attractive receptors have proven to present significant challenges. Among these difficult GPCRs are those whose natural ligands are peptides and proteins. In this review we explain the obstacles faced by GPCR drug disc

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Torrens-Fontanals, Mariona, Tomasz Maciej Stepniewski, David Aranda-García, Adrián Morales-Pastor, Brian Medel-Lacruz, and Jana Selent. "How Do Molecular Dynamics Data Complement Static Structural Data of GPCRs." International Journal of Molecular Sciences 21, no. 16 (2020): 5933. http://dx.doi.org/10.3390/ijms21165933.

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G protein-coupled receptors (GPCRs) are implicated in nearly every physiological process in the human body and therefore represent an important drug targeting class. Advances in X-ray crystallography and cryo-electron microscopy (cryo-EM) have provided multiple static structures of GPCRs in complex with various signaling partners. However, GPCR functionality is largely determined by their flexibility and ability to transition between distinct structural conformations. Due to this dynamic nature, a static snapshot does not fully explain the complexity of GPCR signal transduction. Molecular dyna

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Kozielewicz, Paweł, Konrad Owczarek, and Joanna J. Sajkowska-Kozielewicz. "Class F GPCR – activation mechanism and pharmacology." Farmacja Polska 75, no. 8 (2019): 451–56. http://dx.doi.org/10.32383/farmpol/116110.

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Erlandson, Sarah C., Conor McMahon, and Andrew C. Kruse. "Structural Basis for G Protein–Coupled Receptor Signaling." Annual Review of Biophysics 47, no. 1 (2018): 1–18. http://dx.doi.org/10.1146/annurev-biophys-070317-032931.

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G protein–coupled receptors (GPCRs), which mediate processes as diverse as olfaction and maintenance of metabolic homeostasis, have become the single most effective class of therapeutic drug targets. As a result, understanding the molecular basis for their activity is of paramount importance. Recent technological advances have made GPCR structural biology increasingly tractable, offering views of these receptors in unprecedented atomic detail. Structural and biophysical data have shown that GPCRs function as complex allosteric machines, communicating ligand-binding events through conformationa

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Velazhahan, Vaithish, Ning Ma, Nagarajan Vaidehi, and Christopher G. Tate. "Activation mechanism of the class D fungal GPCR dimer Ste2." Nature 603, no. 7902 (2022): 743–48. http://dx.doi.org/10.1038/s41586-022-04498-3.

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AbstractThe fungal class D1 G-protein-coupled receptor (GPCR) Ste2 has a different arrangement of transmembrane helices compared with mammalian GPCRs and a distinct mode of coupling to the heterotrimeric G protein Gpa1–Ste2–Ste181. In addition, Ste2 lacks conserved sequence motifs such as DRY, PIF and NPXXY, which are associated with the activation of class A GPCRs2. This suggested that the activation mechanism of Ste2 may also differ. Here we determined structures of Saccharomyces cerevisiae Ste2 in the absence of G protein in two different conformations bound to the native agonist α-factor,

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Plante, Ambrose, Derek M. Shore, Giulia Morra, George Khelashvili, and Harel Weinstein. "A Machine Learning Approach for the Discovery of Ligand-Specific Functional Mechanisms of GPCRs." Molecules 24, no. 11 (2019): 2097. http://dx.doi.org/10.3390/molecules24112097.

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G protein-coupled receptors (GPCRs) play a key role in many cellular signaling mechanisms, and must select among multiple coupling possibilities in a ligand-specific manner in order to carry out a myriad of functions in diverse cellular contexts. Much has been learned about the molecular mechanisms of ligand-GPCR complexes from Molecular Dynamics (MD) simulations. However, to explore ligand-specific differences in the response of a GPCR to diverse ligands, as is required to understand ligand bias and functional selectivity, necessitates creating very large amounts of data from the needed large

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Toneatti, Rudy, Jong M. Shin, Urjita H. Shah, et al. "Interclass GPCR heteromerization affects localization and trafficking." Science Signaling 13, no. 654 (2020): eaaw3122. http://dx.doi.org/10.1126/scisignal.aaw3122.

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Membrane trafficking processes regulate G protein–coupled receptor (GPCR) activity. Although class A GPCRs are capable of activating G proteins in a monomeric form, they can also potentially assemble into functional GPCR heteromers. Here, we showed that the class A serotonin 5-HT2A receptors (5-HT2ARs) affected the localization and trafficking of class C metabotropic glutamate receptor 2 (mGluR2) through a mechanism that required their assembly as heteromers in mammalian cells. In the absence of agonists, 5-HT2AR was primarily localized within intracellular compartments, and coexpression of 5-

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Wang, Jialu, Clarice Gareri, and Howard A. Rockman. "G-Protein–Coupled Receptors in Heart Disease." Circulation Research 123, no. 6 (2018): 716–35. http://dx.doi.org/10.1161/circresaha.118.311403.

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GPCRs (G-protein [guanine nucleotide-binding protein]–coupled receptors) play a central physiological role in the regulation of cardiac function in both health and disease and thus represent one of the largest class of surface receptors targeted by drugs. Several antagonists of GPCRs, such as βARs (β-adrenergic receptors) and Ang II (angiotensin II) receptors, are now considered standard of therapy for a wide range of cardiovascular disease, such as hypertension, coronary artery disease, and heart failure. Although the mechanism of action for GPCRs was thought to be largely worked out in the 8

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Patel, Jyoti, Keith M. Channon, and Eileen McNeill. "The Downstream Regulation of Chemokine Receptor Signalling: Implications for Atherosclerosis." Mediators of Inflammation 2013 (2013): 1–12. http://dx.doi.org/10.1155/2013/459520.

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Heterotrimeric G-protein-coupled receptors (GPCRs) are key mediators of intracellular signalling, control numerous physiological processes, and are one of the largest class of proteins to be pharmacologically targeted. Chemokine-induced macrophage recruitment into the vascular wall is an early pathological event in the progression of atherosclerosis. Leukocyte activation and chemotaxis during cell recruitment are mediated by chemokine ligation of multiple GPCRs. Regulation of GPCR signalling is critical in limiting vascular inflammation and involves interaction with downstream proteins such as

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Mattedi, Giulio, Silvia Acosta-Gutiérrez, Timothy Clark, and Francesco Luigi Gervasio. "A combined activation mechanism for the glucagon receptor." Proceedings of the National Academy of Sciences 117, no. 27 (2020): 15414–22. http://dx.doi.org/10.1073/pnas.1921851117.

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We report on a combined activation mechanism for a class B G-protein–coupled receptor (GPCR), the glucagon receptor. By computing the conformational free-energy landscape associated with the activation of the receptor–agonist complex and comparing it with that obtained with the ternary complex (receptor–agonist–G protein) we show that the agonist stabilizes the receptor in a preactivated complex, which is then fully activated upon binding of the G protein. The proposed mechanism contrasts with the generally assumed GPCR activation mechanism, which proceeds through an opening of the intracellul

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Toh, H. "Molecular Phylogenetic Analysis of Class A GPCR." Seibutsu Butsuri 41, supplement (2001): S20. http://dx.doi.org/10.2142/biophys.41.s20_1.

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Harini, K., S. Jayashree, Vikas Tiwari, Sneha Vishwanath, and Ramanathan Sowdhamini. "Ligand Docking Methods to Recognize Allosteric Inhibitors for G-Protein-Coupled Receptors." Bioinformatics and Biology Insights 15 (January 2021): 117793222110377. http://dx.doi.org/10.1177/11779322211037769.

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G-protein-coupled receptors (GPCRs) are membrane proteins which play an important role in many cellular processes and are excellent drug targets. Despite the existence of several US Food and Drug Administration (FDA)-approved GPCR-targeting drugs, there is a continuing challenge of side effects owing to the nonspecific nature of drug binding. We have investigated the diversity of the ligand binding site for this class of proteins against their cognate ligands using computational docking, even if their structures are known already in the ligand-complexed form. The cognate ligand of some of thes

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Zaidman, Nathan A., Viktor N. Tomilin, Naghmeh Hassanzadeh Khayyat, et al. "Adhesion-GPCR Gpr116 (ADGRF5) expression inhibits renal acid secretion." Proceedings of the National Academy of Sciences 117, no. 42 (2020): 26470–81. http://dx.doi.org/10.1073/pnas.2007620117.

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The diversity and near universal expression of G protein-coupled receptors (GPCR) reflects their involvement in most physiological processes. The GPCR superfamily is the largest in the human genome, and GPCRs are common pharmaceutical targets. Therefore, uncovering the function of understudied GPCRs provides a wealth of untapped therapeutic potential. We previously identified an adhesion-class GPCR, Gpr116, as one of the most abundant GPCRs in the kidney. Here, we show that Gpr116 is highly expressed in specialized acid-secreting A-intercalated cells (A-ICs) in the kidney using both imaging an

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Isu, Ugochi H., Shadi A. Badiee, Ehsaneh Khodadadi, and Mahmoud Moradi. "Cholesterol in Class C GPCRs: Role, Relevance, and Localization." Membranes 13, no. 3 (2023): 301. http://dx.doi.org/10.3390/membranes13030301.

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G-protein coupled receptors (GPCRs), one of the largest superfamilies of cell-surface receptors, are heptahelical integral membrane proteins that play critical roles in virtually every organ system. G-protein-coupled receptors operate in membranes rich in cholesterol, with an imbalance in cholesterol level within the vicinity of GPCR transmembrane domains affecting the structure and/or function of many GPCRs, a phenomenon that has been linked to several diseases. These effects of cholesterol could result in indirect changes by altering the mechanical properties of the lipid environment or dire

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Cong, Zhaotong, Yi-Lynn Liang, Qingtong Zhou, et al. "Structural perspective of class B1 GPCR signaling." Trends in Pharmacological Sciences 43, no. 4 (2022): 321–34. http://dx.doi.org/10.1016/j.tips.2022.01.002.

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Tse, Man Tsuey. "Two landmark class B GPCR structures unveiled." Nature Reviews Drug Discovery 12, no. 8 (2013): 579. http://dx.doi.org/10.1038/nrd4082.

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Katritch, Vsevolod, Gustavo Fenalti, Enrique E. Abola, Bryan L. Roth, Vadim Cherezov, and Raymond C. Stevens. "Allosteric sodium in class A GPCR signaling." Trends in Biochemical Sciences 39, no. 5 (2014): 233–44. http://dx.doi.org/10.1016/j.tibs.2014.03.002.

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Xu, Yueming, Yuxia Wang, Yang Wang, et al. "Mutagenesis facilitated crystallization of GLP-1R." IUCrJ 6, no. 6 (2019): 996–1006. http://dx.doi.org/10.1107/s2052252519013496.

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The class B family of G-protein-coupled receptors (GPCRs) has long been a paradigm for peptide hormone recognition and signal transduction. One class B GPCR, the glucagon-like peptide-1 receptor (GLP-1R), has been considered as an anti-diabetes drug target and there are several peptidic drugs available for the treatment of this overwhelming disease. The previously determined structures of inactive GLP-1R in complex with two negative allosteric modulators include ten thermal-stabilizing mutations that were selected from a total of 98 designed mutations. Here we systematically summarize all 98 m

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Guillien, Myriam, Assia Mouhand, Aurélie Fournet, et al. "Structural Insights into the Intrinsically Disordered GPCR C-Terminal Region, Major Actor in Arrestin-GPCR Interaction." Biomolecules 12, no. 5 (2022): 617. http://dx.doi.org/10.3390/biom12050617.

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Arrestin-dependent pathways are a central component of G protein-coupled receptor (GPCRs) signaling. However, the molecular processes regulating arrestin binding are to be further illuminated, in particular with regard to the structural impact of GPCR C-terminal disordered regions. Here, we used an integrated biophysical strategy to describe the basal conformations of the C-terminal domains of three class A GPCRs, the vasopressin V2 receptor (V2R), the growth hormone secretagogue or ghrelin receptor type 1a (GHSR) and the β2-adernergic receptor (β2AR). By doing so, we revealed the presence of

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Civciristov, Srgjan, Andrew M. Ellisdon, Ryan Suderman, et al. "Preassembled GPCR signaling complexes mediate distinct cellular responses to ultralow ligand concentrations." Science Signaling 11, no. 551 (2018): eaan1188. http://dx.doi.org/10.1126/scisignal.aan1188.

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G protein–coupled receptors (GPCRs) are the largest class of cell surface signaling proteins, participate in nearly all physiological processes, and are the targets of 30% of marketed drugs. Typically, nanomolar to micromolar concentrations of ligand are used to activate GPCRs in experimental systems. We detected GPCR responses to a wide range of ligand concentrations, from attomolar to millimolar, by measuring GPCR-stimulated production of cyclic adenosine monophosphate (cAMP) with high spatial and temporal resolution. Mathematical modeling showed that femtomolar concentrations of ligand acti

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König, Caroline, Renè Alqézar, Alfredo Vellido, and Jesús Giraldo. "Reducing the n-gram feature space of class C GPCRs to subtype-discriminating patterns." Journal of Integrative Bioinformatics 11, no. 3 (2014): 99–115. http://dx.doi.org/10.1515/jib-2014-254.

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Summary G protein-coupled receptors (GPCRs) are a large and heterogeneous superfamily of receptors that are key cell players for their role as extracellular signal transmitters. Class C GPCRs, in particular, are of great interest in pharmacology. The lack of knowledge about their full 3-D structure prompts the use of their primary amino acid sequences for the construction of robust classifiers, capable of discriminating their different subtypes. In this paper, we investigate the use of feature selection techniques to build Support Vector Machine (SVM)-based classification models from selected

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Shen, Cangsong, Chunyou Mao, Chanjuan Xu, et al. "Structural basis of GABAB receptor–Gi protein coupling." Nature 594, no. 7864 (2021): 594–98. http://dx.doi.org/10.1038/s41586-021-03507-1.

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AbstractG-protein-coupled receptors (GPCRs) have central roles in intercellular communication1,2. Structural studies have revealed how GPCRs can activate G proteins. However, whether this mechanism is conserved among all classes of GPCR remains unknown. Here we report the structure of the class-C heterodimeric GABAB receptor, which is activated by the inhibitory transmitter GABA, in its active form complexed with Gi1 protein. We found that a single G protein interacts with the GB2 subunit of the GABAB receptor at a site that mainly involves intracellular loop 2 on the side of the transmembrane

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Grundmann, Manuel, Eckhard Bender, Jens Schamberger, and Frank Eitner. "Pharmacology of Free Fatty Acid Receptors and Their Allosteric Modulators." International Journal of Molecular Sciences 22, no. 4 (2021): 1763. http://dx.doi.org/10.3390/ijms22041763.

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The physiological function of free fatty acids (FFAs) has long been regarded as indirect in terms of their activities as educts and products in metabolic pathways. The observation that FFAs can also act as signaling molecules at FFA receptors (FFARs), a family of G protein-coupled receptors (GPCRs), has changed the understanding of the interplay of metabolites and host responses. Free fatty acids of different chain lengths and saturation statuses activate FFARs as endogenous agonists via binding at the orthosteric receptor site. After FFAR deorphanization, researchers from the pharmaceutical i

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Zwier, Jurriaan M., Thomas Roux, Martin Cottet, et al. "A Fluorescent Ligand-Binding Alternative Using Tag-lite® Technology." Journal of Biomolecular Screening 15, no. 10 (2010): 1248–59. http://dx.doi.org/10.1177/1087057110384611.

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G-protein-coupled receptors (GPCRs) are crucial cell surface receptors that transmit signals from a wide range of extracellular ligands. Indeed, 40% to 50% of all marketed drugs are thought to modulate GPCR activity, making them the major class of targets in the drug discovery process. Binding assays are widely used to identify high-affinity, selective, and potent GPCR drugs. In this field, the use of radiolabeled ligands has remained so far the gold-standard method. Here the authors report a less hazardous alternative for high-throughput screening (HTS) applications by the setup of a nonradio

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Fasciani, Irene, Marco Carli, Francesco Petragnano, et al. "GPCRs in Intracellular Compartments: New Targets for Drug Discovery." Biomolecules 12, no. 10 (2022): 1343. http://dx.doi.org/10.3390/biom12101343.

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The architecture of eukaryotic cells is defined by extensive membrane-delimited compartments, which entails separate metabolic processes that would otherwise interfere with each other, leading to functional differences between cells. G protein-coupled receptors (GPCRs) are the largest class of cell surface receptors, and their signal transduction is traditionally viewed as a chain of events initiated from the plasma membrane. Furthermore, their intracellular trafficking, internalization, and recycling were considered only to regulate receptor desensitization and cell surface expression. On the

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Birdsall, Nigel J. M. "Class A GPCR heterodimers: evidence from binding studies." Trends in Pharmacological Sciences 31, no. 11 (2010): 499–508. http://dx.doi.org/10.1016/j.tips.2010.08.003.

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Rowe, Jacob B., Geoffrey J. Taghon, Nicholas J. Kapolka, William M. Morgan, and Daniel G. Isom. "CRISPR-addressable yeast strains with applications in human G protein–coupled receptor profiling and synthetic biology." Journal of Biological Chemistry 295, no. 24 (2020): 8262–71. http://dx.doi.org/10.1074/jbc.ra120.013066.

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Genome stability is essential for engineering cell-based devices and reporter systems. With the advent of CRISPR technology, it is now possible to build such systems by installing the necessary genetic parts directly into an organism's genome. Here, we used this approach to build a set of 10 versatile yeast-based reporter strains for studying human G protein–coupled receptors (GPCRs), the largest class of membrane receptors in humans. These reporter strains contain the necessary genetically encoded parts for studying human GPCR signaling in yeast, as well as four CRISPR-addressable expression

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Dankwah, Kwabena Owusu, Jonathon E. Mohl, Khodeza Begum, and Ming-Ying Leung. "What Makes GPCRs from Different Families Bind to the Same Ligand?" Biomolecules 12, no. 7 (2022): 863. http://dx.doi.org/10.3390/biom12070863.

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G protein-coupled receptors (GPCRs) are the largest class of cell-surface receptor proteins with important functions in signal transduction and often serve as therapeutic drug targets. With the rapidly growing public data on three dimensional (3D) structures of GPCRs and GPCR-ligand interactions, computational prediction of GPCR ligand binding becomes a convincing option to high throughput screening and other experimental approaches during the beginning phases of ligand discovery. In this work, we set out to computationally uncover and understand the binding of a single ligand to GPCRs from se

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Fisher, Gregory W., Margaret H. Fuhrman, Sally A. Adler, Christopher Szent-Gyorgyi, Alan S. Waggoner, and Jonathan W. Jarvik. "Self-Checking Cell-Based Assays for GPCR Desensitization and Resensitization." Journal of Biomolecular Screening 19, no. 8 (2014): 1220–26. http://dx.doi.org/10.1177/1087057114534299.

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G protein–coupled receptors (GPCRs) play stimulatory or modulatory roles in numerous physiological states and processes, including growth and development, vision, taste and olfaction, behavior and learning, emotion and mood, inflammation, and autonomic functions such as blood pressure, heart rate, and digestion. GPCRs constitute the largest protein superfamily in the human and are the largest target class for prescription drugs, yet most are poorly characterized, and of the more than 350 nonolfactory human GPCRs, over 100 are orphans for which no endogenous ligand has yet been convincingly ide

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