Lefkowitz, R. J. Seven transmembrane receptors: something old, something new. Acta Physiol. 190, 9–19 (2007).
Santos, R. et al. A comprehensive map of molecular drug targets. Nat. Rev. Drug Discov. 16, 19–34 (2017).
Article CAS PubMed Google Scholar
Farrens, D. L., Altenbach, C., Yang, K., Hubbell, W. L. & Khorana, H. G. Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science 274, 768–770 (1996).
Article CAS PubMed Google Scholar
Scheerer, P. et al. Crystal structure of opsin in its G-protein-interacting conformation. Nature 455, 497–502 (2008).
Article CAS PubMed Google Scholar
Rasmussen, S. G. F. et al. Crystal structure of the β2 adrenergic receptor–Gs protein complex. Nature 477, 549–557 (2011).
Article CAS PubMed PubMed Central Google Scholar
Flock, T. et al. Universal allosteric mechanism for Gα activation by GPCRs. Nature 524, 173–179 (2015).
Article CAS PubMed PubMed Central Google Scholar
Hauser, A. S. et al. Common coupling map advances GPCR-G protein selectivity. eLife 11, e74107 (2022).
Article CAS PubMed PubMed Central Google Scholar
García-Nafría, J. & Tate, C. G. Structure determination of GPCRs: cryo-EM compared with X-ray crystallography. Biochem. Soc. Trans. 49, 2345 (2021).
Article PubMed PubMed Central Google Scholar
García-Nafría, J. & Tate, C. G. Cryo-EM structures of GPCRs coupled to Gs, Gi and Go. Mol. Cell. Endocrinol. 488, 1–13 (2019).
Du, Y. et al. Assembly of a GPCR–G protein complex. Cell 177, 1232–1242.e11 (2019).
Article CAS PubMed PubMed Central Google Scholar
Heck, M. & Hofmann, K. P. Maximal rate and nucleotide dependence of rhodopsin-catalyzed transducin activation: initial rate analysis based on a double displacement mechanism. J. Biol. Chem. 276, 10000–10009 (2001).
Article CAS PubMed Google Scholar
Scheerer, P. et al. Structural and kinetic modeling of an activating helix switch in the rhodopsin–transducin interface. Proc. Natl Acad. Sci. 106, 10660–10665 (2009).
Article CAS PubMed PubMed Central Google Scholar
Chung, K. Y. et al. Conformational changes in the G protein Gs induced by the β2 adrenergic receptor. Nature 477, 611–615 (2011).
Article CAS PubMed PubMed Central Google Scholar
Gregorio, G. G. et al. Single-molecule analysis of ligand efficacy in β2AR–G-protein activation. Nature 547, 68–73 (2017).
Article CAS PubMed PubMed Central Google Scholar
Okashah, N. et al. Agonist-induced formation of unproductive receptor-G12 complexes. Proc. Natl Acad. Sci. USA 117, 21723–21730 (2020).
Article CAS PubMed PubMed Central Google Scholar
Liu, X. et al. Structural Insights into the process of GPCR–G protein complex formation. Cell 177, 1243–1251.e12 (2019).
Article CAS PubMed PubMed Central Google Scholar
Mahoney, J. P. & Sunahara, R. K. Mechanistic insights into GPCR–G protein interactions. Curr. Opin. Struct. Biol. 41, 247–254 (2016).
Article CAS PubMed PubMed Central Google Scholar
Jang, W., Lu, S., Wu, G. & Lambert, N. A. The role of G protein confirmation in receptor-G protein selectivity. Nat. Chem. Biol. 19, 687–694 (2023).
Article CAS PubMed PubMed Central Google Scholar
Tsutsumi, N. et al. Atypical structural snapshots of human cytomegalovirus GPCR interactions with host G proteins. Sci. Adv. 8, 5442 (2022).
Huang, S. K. et al. Delineating the conformational landscape of the adenosine A2A receptor during G protein coupling. Cell 184, 1884–1894.e14 (2021).
Article CAS PubMed PubMed Central Google Scholar
Huang, S. K. et al. Mapping the conformation landscape of the stimulatory heterotrimeric G protein. Nat. Struct. Mol. Biol. 30, 502–511 (2023).
Article CAS PubMed Google Scholar
Sadler, F. et al. Autoregulation of GPCR signalling through the third intracellular loop A FRET-based approach to probe ICL3 conformation. Nature 615, 734–741 (2023).
Article CAS PubMed PubMed Central Google Scholar
Fleetwood, O., Carlsson, J. & Delemotte, L. Identification of ligand-specific G protein-coupled receptor states and prediction of downstream efficacy via data-driven modeling. eLife 10, e60715 (2021).
Article CAS PubMed PubMed Central Google Scholar
Panel, N. et al. Design of drug efficacy guided by free energy simulations of the β2-adrenoceptor. Angew. Chem. Int. Ed. Engl. 62, e202218959 (2023).
Article CAS PubMed Google Scholar
Robinson, G. A., Butcher, R. W. & Sutherland, E. W. Cyclic AMP. Ann. Rev. Biochem. 37, 149–174 (1968).
Haga, T. et al. Adenylate cyclase permanently uncoupled from hormone receptors in a novel variant of S49 mouse lymphoma cells. Proc. Natl Acad. Sci. USA 74, 2016–2020 (1977).
Article CAS PubMed PubMed Central Google Scholar
Manglik, A., Kobilka, B. K. & Steyaert, J. Nanobodies to study G protein-coupled receptor structure and function. Annu. Rev. Pharmacol. Toxicol. 57, 19–37 (2017).
Article CAS PubMed Google Scholar
Conklin, B. R., Farfel, Z., Lustig, K. D., Julius, D. & Bourne, H. R. Substitution of three amino acids switches receptor specificity of Gqα to that of Giα. Nature 363, 274–276 (1993).
Article CAS PubMed Google Scholar
Flock, T. et al. Selectivity determinants of GPCR–G-protein binding. Nature 545, 317–322 (2017).
Article CAS PubMed PubMed Central Google Scholar
Rose, A. S. et al. Position of transmembrane helix 6 determines receptor G protein coupling specificity. J. Am. Chem. Soc. 136, 11244–11247 (2014).
Article CAS PubMed Google Scholar
Selçuk, B. & Adebali, O. Common and selective signal transduction mechanisms of GPCRs. Prog. Mol. Biol. Transl. Sci. 195, 89–100 (2023).
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