Structure-Function of the G Protein–Coupled Receptor Superfamily

Literature Cited

1. Lagerstrom MC. , Schioth HB. 1. . 2008.. Structural diversity of G protein-coupled receptors and significance for drug discovery. . Nat. Rev. Drug Discov. 7::339–57 [Google Scholar]
2. Fredriksson R. , Lagerstrom MC. , Lundin LG. , Schioth HB. 2. . 2003.. The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints. . Mol. Pharmacol. 63::1256–72 [Google Scholar]
3. Overington JP. , Al-Lazikani B. , Hopkins AL. 3. . 2006.. How many drug targets are there?. Nat. Rev. Drug Discov. 5::993–96 [Google Scholar]
4. Tyndall JD. , Sandilya R. 4. . 2005.. GPCR agonists and antagonists in the clinic. . Med. Chem. 1::405–21 [Google Scholar]
5. Lappano R. , Maggiolini M. 5. . 2011.. G protein-coupled receptors: novel targets for drug discovery in cancer. . Nat. Rev. Drug Discov. 10::47–60 [Google Scholar]
6. Allen JA. , Roth BL. 6. . 2011.. Strategies to discover unexpected targets for drugs active at G protein–coupled receptors. . Annu. Rev. Pharmacol. Toxicol. 51::117–44 [Google Scholar]
7. Valant C. , Lane JR. , Sexton PM. , Christopoulos A. 7. . 2012.. The best of both worlds? Bitopic ortho-steric/allosteric ligands of G protein–coupled receptors. . Annu. Rev. Pharmacol. Toxicol. 52::153–78 [Google Scholar]
8. Reiter E. , Ahn S. , Shukla AK. , Lefkowitz RJ. 8. . 2012.. Molecular mechanism of β-arrestin-biased agonism at seven-transmembrane receptors. . Annu. Rev. Pharmacol. Toxicol. 52::179–97 [Google Scholar]
9. Palczewski K. , Kumasaka T. , Hori T. , Behnke CA. , Motoshima H. 9. , et al. 2000.. Crystal structure of rhodopsin: a G protein-coupled receptor. . Science 289::739–45 [Google Scholar]
10. Schwartz TW. , Frimurer TM. , Holst B. , Rosenkilde MM. , Elling CE. 10. . 2006.. Molecular mechanism of 7TM receptor activation—a global toggle switch model. . Annu. Rev. Pharmacol. Toxicol. 46::481–519 [Google Scholar]
11. Kobilka BK. 11. . 2007.. G protein coupled receptor structure and activation. . Biochim. Biophys. Acta 1768::794–807 [Google Scholar]
12. Rosenbaum DM. , Cherezov V. , Hanson MA. , Rasmussen SG. , Thian FS. 12. , et al. 2007.. GPCR engineering yields high-resolution structural insights into β₂-adrenergic receptor function. . Science 318::1266–73 [Google Scholar]
13. Warne T. , Serrano-Vega MJ. , Baker JG. , Moukhametzianov R. , Edwards PC. 13. , et al. 2008.. Structure of a β₁-adrenergic G-protein-coupled receptor. . Nature 454::486–91 [Google Scholar]
14. Cherezov V. , Hanson MA. , Griffith MT. , Hilgart MC. , Sanishvili R. 13a. , et al. 2009.. Rastering strategy for screening and centering of microcrystal samples of human membrane proteins with a sub-10 micron size X-ray synchrotron beam. . J. R. Soc. Interface 6(Suppl. 5)::S587–97 [Google Scholar]
15. Caffrey M. , Cherezov V. 13b. . 2009.. Crystallizing membrane proteins using lipidic mesophases. . Nat. Protoc. 4::706–31 [Google Scholar]
16. Cherezov V. , Abola E. , Stevens RC. 13c. . 2010.. Recent progress in the structure determination of GPCRs, a membrane protein family with high potential as pharmaceutical targets. . Methods Mol. Biol. 654::141–68 [Google Scholar]
17. Scheerer P. , Park JH. , Hildebrand PW. , Kim YJ. , Krauss N. 14. , et al. 2008.. Crystal structure of opsin in its G-protein-interacting conformation. . Nature 455::497–502 [Google Scholar]
18. Park JH. , Scheerer P. , Hofmann KP. , Choe HW. , Ernst OP. 15. . 2008.. Crystal structure of the ligand-free G-protein-coupled receptor opsin. . Nature 454::183–87 [Google Scholar]
19. Park PS. , Lodowski DT. , Palczewski K. 16. . 2008.. Activation of G protein–coupled receptors: beyond two-state models and tertiary conformational changes. . Annu. Rev. Pharmacol. Toxicol. 48::107–41 [Google Scholar]
20. Standfuss J. , Edwards PC. , D'Antona A. , Fransen M. , Xie G. 17. , et al. 2011.. The structural basis of agonist-induced activation in constitutively active rhodopsin. . Nature 471::656–60 [Google Scholar]
21. Choe HW. , Park JH. , Kim YJ. , Ernst OP. 18. . 2011.. Transmembrane signaling by GPCRs: insight from rhodopsin and opsin structures. . Neuropharmacology 60::52–57 [Google Scholar]
22. Deupi X. , Edwards P. , Singhal A. , Nickle B. , Oprian D. 19. , et al. 2012.. Stabilized G protein binding site in the structure of constitutively active metarhodopsin-II. . Proc. Natl. Acad. Sci. USA 109::119–24 [Google Scholar]
23. Xu F. , Wu H. , Katritch V. , Han GW. , Jacobson KA. 20. , et al. 2011.. Structure of an agonist-bound human A_2A adenosine receptor. . Science 332::322–27 [Google Scholar]
24. Lebon G. , Warne T. , Edwards PC. , Bennett K. , Langmead CJ. 21. , et al. 2011.. Agonist-bound adenosine A_2A receptor structures reveal common features of GPCR activation. . Nature 474::521–25 [Google Scholar]
25. Rasmussen SG. , DeVree BT. , Zou Y. , Kruse AC. , Chung KY. 22. , et al. 2011.. Crystal structure of the β₂ adrenergic receptor–Gs protein complex. . Nature 477::549–55 [Google Scholar]
26. Rasmussen SG. , Choi HJ. , Fung JJ. , Pardon E. , Casarosa P. 23. , et al. 2011.. Structure of a nanobody-stabilized active state of the β₂ adrenoceptor. . Nature 469::175–80 [Google Scholar]
27. Reynolds K. , Abagyan R. , Katritch V. 24. . 2010.. Structure and modeling of GPCRs: implications for drug discovery. . In GPCR Molecular Pharmacology and Drug Targeting: Shifting Paradigms and New Directions, ed. A Gilchrist , pp. 385–433. Hoboken, NJ:: Wiley [Google Scholar]
28. Congreve M. , Langmead CJ. , Mason JS. , Marshall FH. 25. . 2011.. Progress in structure based drug design for G protein-coupled receptors. . J. Med. Chem. 54::4283–311 [Google Scholar]
29. Archbold JK. , Flanagan JU. , Watkins HA. , Gingell JJ. , Hay DL. 26. . 2011.. Structural insights into RAMP modification of secretin family G protein-coupled receptors: implications for drug development. . Trends Pharmacol. Sci. 32::591–600 [Google Scholar]
30. Kniazeff J. , Prezeau L. , Rondard P. , Pin JP. , Goudet C. 27. . 2011.. Dimers and beyond: the functional puzzles of class C GPCRs. . Pharmacol. Ther. 130::9–25 [Google Scholar]
31. Cherezov V. , Rosenbaum DM. , Hanson MA. , Rasmussen SG. , Thian FS. 28. , et al. 2007.. High-resolution crystal structure of an engineered human β₂-adrenergic G protein-coupled receptor. . Science 318::1258–65 [Google Scholar]
32. Shimamura T. , Shiroishi M. , Weyand S. , Tsujimoto H. , Winter G. 29. , et al. 2011.. Structure of the human histamine H₁ receptor complex with doxepin. . Nature 475::65–70 [Google Scholar]
33. Chien EY. , Liu W. , Zhao Q. , Katritch V. , Han GW. 30. , et al. 2010.. Structure of the human dopamine D3 receptor in complex with a D2/D3 selective antagonist. . Science 330::1091–95 [Google Scholar]
34. Haga K. , Kruse AC. , Asada H. , Yurugi-Kobayashi T. , Shiroishi M. 31. , et al. 2012.. Structure of the human M2 muscarinic acetylcholine receptor bound to an antagonist. . Nature 482::547–51 [Google Scholar]
35. Kruse AC. , Hu J. , Pan AC. , Arlow DH. , Rosenbaum DM. 32. , et al. 2012.. Structure and dynamics of the M3 muscarinic acetylcholine receptor. . Nature 482::552–56 [Google Scholar]
36. Hanson MA. , Roth CB. , Jo E. , Griffith MT. , Scott FL. 33. , et al. 2012.. Crystal structure of a lipid G protein-coupled receptor. . Science 335::851–55 [Google Scholar]
37. White JF. , Noinaj N. , Shibata Y. , Love J. , Kloss B. 33a. , et al. 2012.. Structure of the agonist-bound neurotensin receptor. . Nature 490::508–13 [Google Scholar]
38. Wu B. , Chien EY. , Mol CD. , Fenalti G. , Liu W. 34. , et al. 2010.. Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists. . Science 330::1066–71 [Google Scholar]
39. Wu H. , Wacker D. , Mileni M. , Katritch V. , Han GW. 35. , et al. 2012.. Structure of the human κ-opioid receptor in complex with JDTic. . Nature 485::327–32 [Google Scholar]
40. Manglik A. , Kruse AC. , Kobilka TS. , Thian FS. , Mathiesen JM. 36. , et al. 2012.. Crystal structure of the μ-opioid receptor bound to a morphinan antagonist. . Nature 485::321–26 [Google Scholar]
41. Granier S. , Manglik A. , Kruse AC. , Kobilka TS. , Thian FS. 37. , et al. 2012.. Structure of the δ-opioid receptor bound to naltrindole. . Nature 485::400–4 [Google Scholar]
42. Thompson AA. , Liu W. , Chun E. , Katritch V. , Wu H. 38. , et al. 2012.. Structure of the nociceptin/orphanin FQ receptor in complex with a peptide mimetic. . Nature 485::395–99 [Google Scholar]
43. Nakamichi H. , Okada T. 39. . 2006.. Local peptide movement in the photoreaction intermediate of rhodopsin. . Proc. Natl. Acad. Sci. USA 103::12729–34 [Google Scholar]
44. Okada T. , Sugihara M. , Bondar AN. , Elstner M. , Entel P. , Buss V. 40. . 2004.. The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure. . J. Mol. Biol. 342::571–83 [Google Scholar]
45. Hanson MA. , Cherezov V. , Griffith MT. , Roth CB. , Jaakola VP. 41. , et al. 2008.. A specific cholesterol binding site is established by the 2.8 Å structure of the human β₂-adrenergic receptor. . Structure 16::897–905 [Google Scholar]
46. Wacker D. , Fenalti G. , Brown MA. , Katritch V. , Abagyan R. 42. , et al. 2010.. Conserved binding mode of human β₂ adrenergic receptor inverse agonists and antagonist revealed by X-ray crystallography. . J. Am. Chem. Soc. 132::11443–45 [Google Scholar]
47. Moukhametzianov R. , Warne T. , Edwards PC. , Serrano-Vega MJ. , Leslie AG. 43. , et al. 2011.. Two distinct conformations of helix 6 observed in antagonist-bound structures of a β₁-adrenergic receptor. . Proc. Natl. Acad. Sci. USA 108::8228–32 [Google Scholar]
48. Warne T. , Moukhametzianov R. , Baker JG. , Nehme R. , Edwards PC. 44. , et al. 2011.. The structural basis for agonist and partial agonist action on a β₁-adrenergic receptor. . Nature 469::241–44 [Google Scholar]
49. Warne T. , Edwards PC. , Leslie AG. , Tate CG. 45. . 2012.. Crystal structures of a stabilized β₁-adrenoceptor bound to the biased agonists bucindolol and carvedilol. . Structure 20::841–49 [Google Scholar]
50. Dore AS. , Robertson N. , Errey JC. , Ng I. , Hollenstein K. 46. , et al. 2011.. Structure of the adenosine A_2A receptor in complex with ZM241385 and the xanthines XAC and caffeine. . Structure 19::1283–93 [Google Scholar]
51. Jaakola VP. , Griffith MT. , Hanson MA. , Cherezov V. , Chien EY. 47. , et al. 2008.. The 2.6 angstrom crystal structure of a human A_2A adenosine receptor bound to an antagonist. . Science 322::1211–17 [Google Scholar]
52. Kolb P. , Rosenbaum DM. , Irwin JJ. , Fung JJ. , Kobilka BK. , Shoichet BK. 48. . 2009.. Structure-based discovery of β₂-adrenergic receptor ligands. . Proc. Natl. Acad. Sci. USA 106::6843–48 [Google Scholar]
53. Katritch V. , Jaakola VP. , Lane JR. , Lin J. , Ijzerman AP. 49. , et al. 2010.. Structure-based discovery of novel chemotypes for adenosine A_2A receptor antagonists. . J. Med. Chem. 53::1799–809 [Google Scholar]
54. Carlsson J. , Yoo L. , Gao ZG. , Irwin JJ. , Shoichet BK. , Jacobson KA. 50. . 2010.. Structure-based discovery of A_2A adenosine receptor ligands. . J. Med. Chem. 53::3748–55 [Google Scholar]
55. de Graaf C. , Kooistra AJ. , Vischer HF. , Katritch V. , Kuijer M. 51. , et al. 2011.. Crystal structure-based virtual screening for fragment-like ligands of the human histamine H₁ receptor. . J. Med. Chem. 54::8195–206 [Google Scholar]
56. Carlsson J. , Coleman RG. , Setola V. , Irwin JJ. , Fan H. 52. , et al. 2011.. Ligand discovery from a dopamine D₃ receptor homology model and crystal structure. . Nat. Chem. Biol. 7::769–78 [Google Scholar]
57. Mysinger MM. , Weiss DR. , Ziarek JJ. , Gravel S. , Doak AK. 53. , et al. 2012.. Structure-based ligand discovery for the protein-protein interface of chemokine receptor CXCR4. . Proc. Natl. Acad. Sci. USA 109::5517–22 [Google Scholar]
58. Tosh DK. , Phan K. , Gao ZG. , Gakh AA. , Xu F. 54. , et al. 2012.. Optimization of adenosine 5′-carboxamide derivatives as adenosine receptor agonists using structure-based ligand design and fragment-based searching. . J. Med. Chem. 55::4297–308 [Google Scholar]
59. Fredriksson R. , Schioth HB. 55. . 2005.. The repertoire of G-protein-coupled receptors in fully sequenced genomes. . Mol. Pharmacol. 67::1414–25 [Google Scholar]
60. Katritch V. , Cherezov V. , Stevens RC. 56. . 2012.. Diversity and modularity of G protein-coupled receptor structures. . Trends Pharmacol. Sci. 33::17–27 [Google Scholar]
61. Kufareva I. , Rueda M. , Katritch V. , Stevens RC. , Abagyan R. 57. . 2011.. Status of GPCR modeling and docking as reflected by community-wide GPCR Dock 2010 assessment. . Structure 19::1108–26 [Google Scholar]
62. Katritch V. , Kufareva I. , Abagyan R. 58. . 2011.. Structure based prediction of subtype-selectivity for adenosine receptor antagonists. . Neuropharmacology 60::108–15 [Google Scholar]
63. Wheatley M. , Wootten D. , Conner M. , Simms J. , Kendrick R. 59. , et al. 2011.. Lifting the lid on G-protein-coupled receptors: the role of extracellular loops. . Br. J. Pharmacol. 165::1688–703 [Google Scholar]
64. Ballesteros JA. , Weinstein H. 60. . 1995.. Integrated methods for the construction of three dimensional models and computational probing of structure-function relations in G-protein coupled receptors. . Methods Neurosci. 25::366–428 [Google Scholar]
65. Strotmann R. , Schrock K. , Boselt I. , Staubert C. , Russ A. , Schoneberg T. 61. . 2011.. Evolution of GPCR: change and continuity. . Mol. Cell. Endocrinol. 331::170–78 [Google Scholar]
66. Seifert R. , Wenzel-Seifert K. 62. . 2002.. Constitutive activity of G-protein-coupled receptors: cause of disease and common property of wild-type receptors. . Naunyn-Schmiedeberg's Arch. Pharmacol. 366::381–416 [Google Scholar]
67. Kobilka BK. , Deupi X. 63. . 2007.. Conformational complexity of G-protein-coupled receptors. . Trends Pharmacol. Sci. 28::397–406 [Google Scholar]
68. Nygaard R. , Frimurer TM. , Holst B. , Rosenkilde MM. , Schwartz TW. 64. . 2009.. Ligand binding and micro-switches in 7TM receptor structures. . Trends Pharmacol. Sci. 30::249–59 [Google Scholar]
69. Liu JJ. , Horst R. , Katritch V. , Stevens RC. , Wuthrich K. 65. . 2012.. Biased signaling pathways in β₂-adrenergic receptor characterized by ¹⁹F-NMR. . Science 335::1106–10 [Google Scholar]
70. Vogel R. , Mahalingam M. , Ludeke S. , Huber T. , Siebert F. , Sakmar TP. 66. . 2008.. Functional role of the “ionic lock”—an interhelical hydrogen-bond network in family A heptahelical receptors. . J. Mol. Biol. 380::648–55 [Google Scholar]
71. Vanni S. , Neri M. , Tavernelli I. , Rothlisberger U. 67. . 2009.. Observation of “ionic lock” formation in molecular dynamics simulations of wild-type β₁ and β₂ adrenergic receptors. . Biochemistry 48::4789–97 [Google Scholar]
72. Warne T. , Serrano-Vega MJ. , Tate CG. , Schertler GF. 68. . 2009.. Development and crystallization of a minimal thermostabilised G protein-coupled receptor. . Protein Expr. Purif. 65::204–13 [Google Scholar]
73. Li B. , Nowak NM. , Kim SK. , Jacobson KA. , Bagheri A. 69. , et al. 2005.. Random mutagenesis of the M₃ muscarinic acetylcholine receptor expressed in yeast: identification of second-site mutations that restore function to a coupling-deficient mutant M₃ receptor. . J. Biol. Chem. 280::5664–75 [Google Scholar]
74. Biebermann H. , Schöneberg T. , Schulz A. , Krause G. , Grüters A. 70. , et al. 1998.. A conserved tyrosine residue (Y601) in transmembrane domain 5 of the human thyrotropin receptor serves as a molecular switch to determine G-protein coupling. . FASEB J 12::1461–71 [Google Scholar]
75. Gao ZG. , Jacobson KA. 71. . 2006.. Keynote review: allosterism in membrane receptors. . Drug Discov. Today 11::191–202 [Google Scholar]
76. Kenakin T. , Miller LJ. 72. . 2010.. Seven transmembrane receptors as shapeshifting proteins: the impact of allosteric modulation and functional selectivity on new drug discovery. . Pharmacol. Rev. 62::265–304 [Google Scholar]
77. Keov P. , Sexton PM. , Christopoulos A. 73. . 2011.. Allosteric modulation of G protein-coupled receptors: a pharmacological perspective. . Neuropharmacology 60::24–35 [Google Scholar]
78. Whalen EJ. , Rajagopal S. , Lefkowitz RJ. 74. . 2011.. Therapeutic potential of β-arrestin- and G protein-biased agonists. . Trends Mol. Med. 17::126–39 [Google Scholar]
79. Thompson MD. , Cole DE. , Jose PA. 74a. . 2008.. Pharmacogenomics of G protein-coupled receptor signaling: insights from health and disease. . Methods Mol. Biol. 448::77–107 [Google Scholar]
80. Ritter SL. , Hall RA. 74b. . 2009.. Fine-tuning of GPCR activity by receptor-interacting proteins. . Nat. Rev. Mol. Cell Biol. 10::819–30 [Google Scholar]
81. Chini B. , Parenti M. 74c. . 2009.. G-protein-coupled receptors, cholesterol and palmitoylation: facts about fats. . J. Mol. Endocrinol. 42::371–79 [Google Scholar]
82. Shi L. , Liapakis G. , Xu R. , Guarnieri F. , Ballesteros JA. , Javitch JA. 75. . 2002.. β₂ adrenergic receptor activation: modulation of the proline kink in transmembrane 6 by a rotamer toggle switch. . J. Biol. Chem. 277::40989–96 [Google Scholar]
83. Katritch V. , Reynolds KA. , Cherezov V. , Hanson MA. , Roth CB. 76. , et al. 2009.. Analysis of full and partial agonists binding to β₂-adrenergic receptor suggests a role of transmembrane helix V in agonist-specific conformational changes. . J. Mol. Recognit. 22::307–18 [Google Scholar]
84. Vilar S. , Karpiak J. , Berk B. , Costanzi S. 77. . 2011.. In silico analysis of the binding of agonists and blockers to the β₂-adrenergic receptor. . J. Mol. Graph. Model. 29::809–17 [Google Scholar]
85. Escribá PV. , Wedegaertner PB. , Goñi FM. , Vögler O. 78. . 2007.. Lipid-protein interactions in GPCR-associated signaling. . Biochim. Biophys. Acta 1768::836–52 [Google Scholar]
86. Liu W. , Chun E. , Thompson A. , Chubukov P. , Xu F. 79. , et al. 2012.. Structural basis for allosteric regulation of GPCRs by sodium ions. . Science 337::232–36 [Google Scholar]
87. Pert CB. , Pasternak G. , Snyder SH. 80. . 1973.. Opiate agonists and antagonists discriminated by receptor binding in brain. . Science 182::1359–61 [Google Scholar]
88. Jiang Q. , Lee BX. , Glashofer M. , van Rhee AM. , Jacobson KA. 81. . 1997.. Mutagenesis reveals structure-activity parallels between human A_2A adenosine receptors and biogenic amine G protein-coupled receptors. . J. Med. Chem. 40::2588–95 [Google Scholar]
89. Parker MS. , Wong YY. , Parker SL. 82. . 2008.. An ion-responsive motif in the second transmembrane segment of rhodopsin-like receptors. . Amino Acids 35::1–15 [Google Scholar]
90. Selent J. , Sanz F. , Pastor M. , De Fabritiis G. 83. . 2010.. Induced effects of sodium ions on dopaminergic G-protein coupled receptors. . PLoS Comput. Biol. 6:: e1000884 [Google Scholar]
91. Milligan G. 84. . 2009.. G protein-coupled receptor hetero-dimerization: contribution to pharmacology and function. . Br. J. Pharmacol. 158::5–14 [Google Scholar]
92. Maurice P. , Kamal M. , Jockers R. 85. . 2011.. Asymmetry of GPCR oligomers supports their functional relevance. . Trends Pharmacol. Sci. 32::514–20 [Google Scholar]
93. Kaczor AA. , Selent J. 86. . 2011.. Oligomerization of G protein-coupled receptors: biochemical and biophysical methods. . Curr. Med. Chem. 18::4606–34 [Google Scholar]
94. Selent J. , Kaczor AA. 87. . 2011.. Oligomerization of G protein-coupled receptors: computational methods. . Curr. Med. Chem. 18::4588–605 [Google Scholar]
95. Khelashvili G. , Dorff K. , Shan J. , Camacho-Artacho M. , Skrabanek L. 88. , et al. 2010.. GPCR-OKB: the G protein coupled receptor oligomer knowledge base. . Bioinformatics 26::1804–5 [Google Scholar]
96. Salom D. , Lodowski DT. , Stenkamp RE. , Le Trong I. , Golczak M. 89. , et al. 2006.. Crystal structure of a photoactivated deprotonated intermediate of rhodopsin. . Proc. Natl. Acad. Sci. USA 103::16123–28 [Google Scholar]
97. Taylor MS. , Fung HK. , Rajgaria R. , Filizola M. , Weinstein H. , Floudas CA. 90. . 2008.. Mutations affecting the oligomerization interface of G-protein-coupled receptors revealed by a novel de novo protein design framework. . Biophys. J. 94::2470–81 [Google Scholar]
98. Suda K. , Filipek S. , Palczewski K. , Engel A. , Fotiadis D. 91. . 2004.. The supramolecular structure of the GPCR rhodopsin in solution and native disc membranes. . Mol. Membr. Biol. 21::435–46 [Google Scholar]
99. Mancia F. , Assur Z. , Herman AG. , Siegel R. , Hendrickson WA. 92. . 2008.. Ligand sensitivity in dimeric associations of the serotonin 5HT2c receptor. . EMBO Rep. 9::363–69 [Google Scholar]
100. Guo W. , Urizar E. , Kralikova M. , Mobarec JC. , Shi L. 93. , et al. 2008.. Dopamine D2 receptors form higher order oligomers at physiological expression levels. . EMBO J. 27::2293–304 [Google Scholar]
101. Guo W. , Shi L. , Filizola M. , Weinstein H. , Javitch JA. 94. . 2005.. Crosstalk in G protein-coupled receptors: Changes at the transmembrane homodimer interface determine activation. . Proc. Natl. Acad. Sci. USA 102::17495–500 [Google Scholar]
102. Lopez-Gimenez JF. , Canals M. , Pediani JD. , Milligan G. 95. . 2007.. The α_1b-adrenoceptor exists as a higher-order oligomer: Effective oligomerization is required for receptor maturation, surface delivery, and function. . Mol. Pharmacol. 71::1015–29 [Google Scholar]
103. Milligan G. , Pediani JD. , Canals M. , Lopez-Gimenez JF. 96. . 2006.. Oligomeric structure of the α_1b-adrenoceptor: comparisons with rhodopsin. . Vision Res. 46::4434–41 [Google Scholar]
104. Klco JM. , Lassere TB. , Baranski TJ. 97. . 2003.. C5a receptor oligomerization: I. Disulfide trapping reveals oligomers and potential contact surfaces in a G protein-coupled receptor. . J. Biol. Chem. 278::35345–53 [Google Scholar]
105. Hernanz-Falcon P. , Rodriguez-Frade JM. , Serrano A. , Juan D. , del Sol A. 98. , et al. 2004.. Identification of amino acid residues crucial for chemokine receptor dimerization. . Nat. Immunol. 5::216–23 [Google Scholar]
106. Fotiadis D. , Liang Y. , Filipek S. , Saperstein DA. , Engel A. , Palczewski K. 99. . 2004.. The G protein-coupled receptor rhodopsin in the native membrane. . FEBS Lett. 564::281–88 [Google Scholar]
107. Yao XJ. , Velez Ruiz G. , Whorton MR. , Rasmussen SG. , DeVree BT. 100. , et al. 2009.. The effect of ligand efficacy on the formation and stability of a GPCR-G protein complex. . Proc. Natl. Acad. Sci. USA 106::9501–6 [Google Scholar]
108. Deupi X. , Kobilka BK. 101. . 2010.. Energy landscapes as a tool to integrate GPCR structure, dynamics, and function. . Physiology 25::293–303 [Google Scholar]
109. Goblyos A. , Ijzerman AP. 102. . 2011.. Allosteric modulation of adenosine receptors. . Biochim. Biophys. Acta 1808::1309–18 [Google Scholar]
110. Gether U. , Lin S. , Kobilka BK. 103. . 1995.. Fluorescent labeling of purified β₂ adrenergic receptor: evidence for ligand-specific conformational changes. . J. Biol. Chem. 270::28268–75 [Google Scholar]
111. Ghanouni P. , Gryczynski Z. , Steenhuis JJ. , Lee TW. , Farrens DL. 104. , et al. 2001.. Functionally different agonists induce distinct conformations in the G protein coupling domain of the β₂ adrenergic receptor. . J. Biol. Chem. 276::24433–36 [Google Scholar]
112. Altenbach C. , Kusnetzow AK. , Ernst OP. , Hofmann KP. , Hubbell WL. 105. . 2008.. High-resolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation. . Proc. Natl. Acad. Sci. USA 105::7439–44 [Google Scholar]
113. Lodowski DT. , Palczewski K. , Miyagi M. 106. . 2010.. Conformational changes in the G protein-coupled receptor rhodopsin revealed by histidine hydrogen-deuterium exchange. . Biochemistry 49::9425–27 [Google Scholar]
114. West GM. , Chien EY. , Katritch V. , Gatchalian J. , Chalmers MJ. 107. , et al. 2011.. Ligand-dependent perturbation of the conformational ensemble for the GPCR β₂ adrenergic receptor revealed by HDX. . Structure 19::1424–32 [Google Scholar]
115. Chung KY. , Rasmussen SG. , Liu T. , Li S. , DeVree BT. 108. , et al. 2011.. Conformational changes in the G protein Gs induced by the β₂adrenergic receptor. . Nature 477::611–15 [Google Scholar]
116. Bokoch MP. , Zou Y. , Rasmussen SG. , Liu CW. , Nygaard R. 109. , et al. 2010.. Ligand-specific regulation of the extracellular surface of a G-protein-coupled receptor. . Nature 463::108–12 [Google Scholar]
117. Kim TY. , Uji-i H. , Moller M. , Muls B. , Hofkens J. , Alexiev U. 110. . 2009.. Monitoring the interaction of a single G-protein key binding site with rhodopsin disk membranes upon light activation. . Biochemistry 48::3801–3 [Google Scholar]
118. Bockenhauer S. , Furstenberg A. , Yao XJ. , Kobilka B. , Moerner WE. 111. . 2011.. Conformational dynamics of single G protein-coupled receptors in solution. . J. Phys. Chem. B 115::13328–38 [Google Scholar]
119. Rahmeh R. , Damian M. , Cottet M. , Orcel H. , Mendre C. 112. , et al. 2012.. Structural insights into biased G protein-coupled receptor signaling revealed by fluorescence spectroscopy. . Proc. Natl. Acad. Sci. USA 109::6733–38 [Google Scholar]
120. Nobles KN. , Xiao K. , Ahn S. , Shukla AK. , Lam CM. 113. , et al. 2011.. Distinct phosphorylation sites on the β₂-adrenergic receptor establish a barcode that encodes differential functions of β-arrestin. . Sci. Signal. 4::ra51 [Google Scholar]
121. Rosenbaum DM. , Zhang C. , Lyons JA. , Holl R. , Aragao D. 114. , et al. 2011.. Structure and function of an irreversible agonist-β₂ adrenoceptor complex. . Nature 469::236–40 [Google Scholar]
122. Dror RO. , Pan AC. , Arlow DH. , Borhani DW. , Maragakis P. 115. , et al. 2011.. Pathway and mechanism of drug binding to G-protein-coupled receptors. . Proc. Natl. Acad. Sci. USA 108::13118–23 [Google Scholar]
123. Hino T. , Arakawa T. , Iwanari H. , Yurugi-Kobayashi T. , Ikeda-Suno C. 116. , et al. 2012.. G-protein-coupled receptor inactivation by an allosteric inverse-agonist antibody. . Nature 482::237–40 [Google Scholar]
124. Congreve M. , Andrews SP. , Dore AS. , Hollenstein K. , Hurrell E. 117. , et al. 2012.. Discovery of 1,2,4-triazine derivatives as adenosine A_2A antagonists using structure based drug design. . J. Med. Chem. 55::1898–903 [Google Scholar]
125. Rasmussen SG. , Choi HJ. , Rosenbaum DM. , Kobilka TS. , Thian FS. 118. , et al. 2007.. Crystal structure of the human β₂ adrenergic G-protein-coupled receptor. . Nature 450::383–87 [Google Scholar]
126. Li J. , Edwards PC. , Burghammer M. , Villa C. , Schertler GF. 119. . 2004.. Structure of bovine rhodopsin in a trigonal crystal form. . J. Mol. Biol. 343::1409–38 [Google Scholar]