Activation of G Protein-Coupled Receptors

Advances in Protein Chemistry

Volumn 74, Issue , 2007, Pages 137-166

  Deupi, Xavier ^a   Kobilka, Brian ^a  

^a STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR; RHODOPSIN;

AMINO TERMINAL SEQUENCE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; ELECTRON SPIN RESONANCE; ENERGY; FLUORESCENCE SPECTROSCOPY; HUMAN; KINETICS; LIGAND BINDING; PHYSIOLOGY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STRUCTURE; REVIEW; SIGNAL TRANSDUCTION; STRUCTURE ANALYSIS;

HETEROTRIMERIC GTP-BINDING PROTEINS; PROTEIN CONFORMATION; RECEPTORS, G-PROTEIN-COUPLED;

EID: 34548438468     PISSN: 00653233     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-3233(07)74004-4     Document Type: Review

References (102)

1. Alewijnse A.E., Timmerman H., Jacobs E.H., Smit M.J., Roovers E., Cotecchia S., and Leurs R. The effect of mutations in the dry motif on the constitutive activity and structural instability of the histamine H(2) receptor. Mol. Pharmacol. 57 (2000) 890-898
2. Altenbach C., Cai K., Khorana H.G., and Hubbell W.L. Structural features and light-dependent changes in the sequence 306-322 extending from helix VII to the palmitoylation sites in rhodopsin: A site-directed spin-labeling study. Biochemistry 38 (1999) 7931-7937
3. Altenbach C., Klein-Seetharaman J., Hwa J., Khorana H.G., and Hubbell W.L. Structural features and light-dependent changes in the sequence 59-75 connecting helices I and II in rhodopsin: A site-directed spin-labeling study. Biochemistry 38 (1999) 7945-7949
4. Altenbach C., Klein-Seetharaman J., Cai K., Khorana H.G., and Hubbell W.L. Structure and rhodopsin: Mapping light-dependent changes in distance between residue 316 in helix 8 and residues in the sequence 60-75, covering the cytoplasmic end of helices TM1 and TM2 and their connection loop CL1. Biochemistry 40 (2001) 15493-15500
5. Angers S., Salahpour A., and Bouvier M. Dimerization: An emerging concept for G protein-coupled receptor ontogeny and function. Annu. Rev. Pharmacol. Toxicol. 42 (2002) 409-435
6. Archer E., Maigret B., Escrieut C., Pradayrol L., and Fourmy D. Rhodopsin crystal: New template yielding realistic models of G-protein-coupled receptors?. Trends Pharmacol. Sci. 24 (2003) 36-40
7. Arnis S., Fahmy K., Hofmann K.P., and Sakmar T.P. A conserved carboxylic acid group mediates light-dependent proton uptake and signaling by rhodopsin. J. Biol. Chem. 269 (1994) 23879-23881
8. Attwood T.K., and Findlay J.B. Fingerprinting G-protein-coupled receptors. Protein Eng. 7 (1994) 195-203
9. Azzi M., Charest P.G., Angers S., Rousseau G., Kohout T., Bouvier M., and Pineyro G. Beta-arrestin-mediated activation of MAPK by inverse agonists reveals distinct active conformations for G protein-coupled receptors. Proc. Natl. Acad. Sci. USA 100 (2003) 11406-11411
10. Baker J.G., Hall I.P., and Hill S.J. Agonist actions of "beta-blockers" provide evidence for two agonist activation sites or conformations of the human beta1-adrenoceptor. Mol. Pharmacol. 63 (2003) 1312-1321
11. Balmforth A.J., Lee A.J., Warburton P., Donnelly D., and Ball S.G. The conformational change responsible for AT1 receptor activation is dependent upon two juxtaposed asparagine residues on transmembrane helices III and VII. J. Biol. Chem. 272 (1997) 4245-4251
12. Baneres J.L., and Parello J. Structure-based analysis of GPCR function: Evidence for a novel pentameric assembly between the dimeric leukotriene B4 receptor BLT1 and the G-protein. J. Mol. Biol. 329 (2003) 815-829
13. Ballesteros J.A., Jensen A.D., Liapakis G., Rasmussen S.G., Shi L., Gether U., and Javitch J.A. Activation of the beta 2-adrenergic receptor involves disruption of an ionic lock between the cytoplasmic ends of transmembrane segments 3 and 6. J. Biol. Chem. 276 (2001) 29171-29177
14. Ballesteros J.A., Shi L., and Javitch J.A. Structural mimicry in G protein-coupled receptors: Implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors. Mol. Pharmacol. 60 (2001) 1-19
15. Bulenger S., Marullo S., and Bouvier M. Emerging role of homo- and heterodimerization in G-protein-coupled receptor biosynthesis and maturation. Trends Pharmacol. Sci. 26 (2005) 131-137
16. Cerione R.A., Staniszewski C., Benovic J.L., Lefkowitz R.J., Caron M.G., Gierschik P., Somers R., Spiegel A.M., Codina J., and Birnbaumer L. Specificity of the functional interactions of the β-adrenergic receptor and rhodopsin with guanine nucleotide regulatory proteins reconstituted in phospholipid vesicles. J. Biol. Chem. 260 (1985) 1493-1500
17. Del Carmine R., Molinari P., Sbraccia M., Ambrosio C., and Costa T. "Induced-fit" mechanism for catecholamine binding to the beta2-adrenergic receptor. Mol. Pharmacol. 66 (2004) 356-363
18. Devi L.A. Heterodimerization of G-protein-coupled receptors: Pharmacology, signaling and trafficking. Trends Pharmacol. Sci. 22 (2001) 532-537
19. Dunham T.D., and Farrens D.L. Conformational changes in rhodopsin. Movement of helix f detected by site-specific chemical labeling and fluorescence spectroscopy. J. Biol. Chem. 274 (1999) 1683-1690
20. Farrens D.L., Altenbach C., Yang K., Hubbell W.L., and Khorana H.G. Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science 274 (1996) 768-770
21. Fredriksson R., Lagerstrom M.C., Lundin L.G., and Schioth H.B. The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints. Mol. Pharmacol. 63 (2003) 1256-1272
22. Gaborik Z., Jagadeesh G., Zhang M., Spat A., Catt K.J., and Hunyady L. The role of a conserved region of the second intracellular loop in AT1 angiotensin receptor activation and signaling. Endocrinology 144 (2003) 2220-2228
23. Gether U., Ballesteros J.A., Seifert R., Sanders-Bush E., Weinstein H., and Kobilka B.K. Structural instability of a constitutively active G protein-coupled receptor. Agonist-independent activation due to conformational flexibility. J. Biol. Chem. 272 (1997) 2587-2590
24. Gether U., Lin S., Ghanouni P., Ballesteros J.A., Weinstein H., and Kobilka B.K. Agonists induce conformational changes in transmembrane domains III and VI of the beta2 adrenoceptor. EMBO J. 16 (1997) 6737-6747
25. Ghanouni P., Schambye H., Seifert R., Lee T.W., Rasmussen S.G., Gether U., and Kobilka B.K. The effect of pH on beta(2) adrenoceptor function. Evidence for protonation-dependent activation. J. Biol. Chem. 275 (2000) 3121-3127
26. Ghanouni P., Gryczynski Z., Steenhuis J.J., Lee T.W., Farrens D.L., Lakowicz J.R., and Kobilka B.K. Functionally different agonists induce distinct conformations in the G protein coupling domain of the beta 2 adrenergic receptor. J. Biol. Chem. 276 (2001) 24433-24436
27. Ghanouni P., Steenhuis J.J., Farrens D.L., and Kobilka B.K. Agonist-induced conformational changes in the G-protein-coupling domain of the beta 2 adrenergic receptor. Proc. Natl. Acad. Sci. USA 98 (2001) 5997-6002
28. Greasley P.J., Fanelli F., Rossier O., Abuin L., and Cotecchia S. Mutagenesis and modelling of the alpha(1b)-adrenergic receptor highlight the role of the helix 3/helix 6 interface in receptor activation. Mol. Pharmacol. 61 (2002) 1025-1032
29. Howard A.D., McAllister G., Feighner S.D., Liu Q., Nargund R.P., Van der Ploeg L.H., and Patchett A.A. Orphan G-protein-coupled receptors and natural ligand discovery. Trends Pharmacol. Sci. 22 (2001) 132-140
30. Hubbell W.L., Altenbach C., Hubbell C.M., and Khorana H.G. Rhodopsin structure, dynamics, and activation: A perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking. Adv. Protein Chem. 63 (2003) 243-290
31. Javitch J.A. The ants go marching two by two: Oligomeric structure of G-protein-coupled receptors. Mol. Pharmacol. 66 (2004) 1077-1082
32. Javitch J.A., Fu D., Liapakis G., and Chen J. Constitutive activation of the beta2 adrenergic receptor alters the orientation of its sixth membrane-spanning segment. J. Biol. Chem. 272 (1997) 18546-18549
33. Ji T.H., Grossmann M., and Ji I. G protein-coupled receptors. I. Diversity of receptor-ligand interactions. J. Biol. Chem. 273 (1998) 17299-17302
34. Jongejan A., Bruysters M., Ballesteros J.A., Haaksma E., Bakker R.A., Pardo L., and Leurs R. Linking agonist binding to histamine H1 receptor activation. Nat. Chem. Biol. 1 (2001) 98-103
35. Kenakin T. Inverse, protean, and ligand-selective agonism: Matters of receptor conformation. FASEB J. 15 (2001) 598-611
36. Kenakin T. Efficacy at G-protein-coupled receptors. Nat. Rev. Drug Discov. 1 (2002) 103-110
37. Kenakin T. Ligand-selective receptor conformations revisited: The promise and the problem. Trends Pharmacol. Sci. 24 (2003) 346-354
38. Kim J.M., Altenbach C., Thurmond R.L., Khorana H.G., and Hubbell W.L. Structure and function in rhodopsin: Rhodopsin mutants with a neutral amino acid at E134 have a partially activated conformation in the dark state. Proc. Natl. Acad. Sci. USA 94 (1997) 14273-14278
39. Knoflach F., Mutel V., Jolidon S., Kew J.N., Malherbe P., Vieira E., Wichmann J., and Kemp J.A. Positive allosteric modulators of metabotropic glutamate 1 receptor: Characterization, mechanism of action, and binding site. Proc. Natl. Acad. Sci. USA 98 (2001) 13402-13407
40. Kobilka B.K., Kobilka T.S., Daniel K., Regan J.W., Caron M.G., and Lefkowitz R.J. Chimeric alpha 2-,beta 2-adrenergic receptors: Delineation of domains involved in effector coupling and ligand binding specificity. Science 240 (1988) 1310-1316
41. Kolakowski Jr. L.F. Gcrdb: A G-protein-coupled receptor database. Receptors Channels 2 (1994) 1-7
42. Krebs A., Edwards P.C., Villa C., Li J., and Schertler G.F. The three-dimensional structure of bovine rhodopsin determined by electron cryomicroscopy. J. Biol. Chem. 278 (2003) 50217-50225
43. Kudo M., Osuga Y., Kobilka B.K., and Hsueh A.J.W. Transmembrane regions V and VI of the human luteinizing hormone receptor are required for constitutive activation by a mutation in the third intracellular loop. J. Biol. Chem. 271 (1996) 22470-22478
44. Kunishima N., Shimada Y., Tsuji Y., Sato T., Yamamoto M., Kumasaka T., Nakanishi S., Jingami H., and Morikawa K. Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor. Nature 407 (2000) 971-977
45. Leff P. The two-state model of receptor activation [see comments]. Trends Pharmacol. Sci. 16 (1995) 89-97
46. Lefkowitz R.J., and Shenoy S.K. Transduction of receptor signals by beta-arrestins. Science 308 (2005) 512-517
47. Lefkowitz R.J., Cotecchia S., Samama P., and Costa T. Constitutive activity of receptors coupled to guanine nucleotide regulatory proteins. Trends Pharmacol. Sci. 14 (1993) 303-307
48. Li J., Edwards P.C., Burghammer M., Villa C., and Schertler G.F. Structure of bovine rhodopsin in a trigonal crystal form. J. Mol. Biol. 343 (2004) 1409-1438
49. Liang Y., Fotiadis D., Filipek S., Saperstein D.A., Palczewski K., and Engel A. Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes. J. Biol. Chem. 278 (2003) 21655-21662
50. Liapakis G., Ballesteros J.A., Papachristou S., Chan W.C., Chen X., and Javitch J.A. The forgotten serine. A critical role for ser-2035.42 in ligands binding to and activation of the beta 2-adrenergic receptor. J. Biol. Chem. 275 (2000) 37779-37788
51. Liapakis G., Chan W.C., Papadokostaki M., and Javitch J.A. Synergistic contributions of the functional groups of epinephrine to its affinity and efficacy at the beta2 adrenergic receptor. Mol. Pharmacol. 65 (2004) 1181-1190
52. Liggett S.B., Caron M.G., Lefkowitz R.J., and Hnatowich M. Coupling of a mutated form of the human beta 2-adrenergic receptor to Gi and Gs. Requirement for multiple cytoplasmic domains in the coupling process. J. Biol. Chem. 266 (1991) 4816-4821
53. Lin S.W., and Sakmar T.P. Specific tryptophan UV-absorbance changes are probes of the transition of rhodopsin to its active state. Biochemistry 35 (1996) 11149-11159
54. Luttrell L.M., and Lefkowitz R.J. The role of beta-arrestins in the termination and transduction of G-protein-coupled receptor signals. J. Cell. Sci. 115 (2002) 455-465
55. McLean A.J., Zeng F.Y., Behan D., Chalmers D., and Milligan G. Generation and analysis of constitutively active and physically destabilized mutants of the human beta(1)-adrenoceptor. Mol. Pharmacol. 62 (2002) 747-755
56. Mesnier D., and Baneres J.L. Cooperative conformational changes in a G-protein-coupled receptor dimer, the leukotriene b(4) receptor blt1. J. Biol. Chem. 279 (2004) 49664-49670
57. Mirzadegan T., Benko G., Filipek S., and Palczewski K. Sequence analyses of G-protein-coupled receptors: Similarities to rhodopsin. Biochemistry 42 (2003) 2759-2767
58. Nie J., and Lewis D.L. Structural domains of the CB1 cannabinoid receptor that contribute to constitutive activity and G-protein sequestration. J. Neurosci. 21 (2001) 8758-8764
59. Nishi S., Nakabayashi K., Kobilka B., and Hsueh A.J. The ectodomain of the luteinizing hormone receptor interacts with exoloop 2 to constrain the transmembrane region: Studies using chimeric human and fly receptors. J. Biol. Chem. 277 (2002) 3958-3964
60. Noda K., Feng Y.H., Liu X.P., Saad Y., Husain A., and Karnik S.S. The active state of the AT1 angiotensin receptor is generated by angiotensin II induction. Biochemistry 35 (1996) 16435-16442
61. 2-adrenergic receptor. Localization of regions involved in G protein-receptor coupling. J. Biol. Chem. 263 (1988) 15985-15992
62. Okada T. X-ray crystallographic studies for ligand-protein interaction changes in rhodopsin. Biochem. Soc. Trans. 32 (2004) 738-741
63. Okada T., Le Trong I., Fox B.A., Behnke C.A., Stenkamp R.E., and Palczewski K. X-ray diffraction analysis of three-dimensional crystals of bovine rhodopsin obtained from mixed micelles. J. Struct. Biol. 130 (2000) 73-80
64. Okada T., Fujiyoshi Y., Silow M., Navarro J., Landau E.M., and Shichida Y. Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography. Proc. Natl. Acad. Sci. USA 99 (2002) 5982-5987
65. Okada T., Sugihara M., Bondar A.N., Elstner M., Entel P., and Buss V. The retinal conformation and its environment in rhodopsin in light of a new 2.2 a crystal structure. J. Mol. Biol. 342 (2004) 571-583
66. Palanche T., Ilien B., Zoffmann S., Reck M.P., Bucher B., Edelstein S.J., and Galzi J.L. The neurokinin a receptor activates calcium and camp responses through distinct conformational states. J. Biol. Chem. 276 (2001) 34853-34861
67. Palczewski K., Kumasaka T., Hori T., Behnke C.A., Motoshima H., Fox B.A., Le Trong I., Teller D.C., Okada T., Stenkamp R.E., Yamamoto M., and Miyano M. Crystal structure of rhodopsin: A G protein-coupled receptor [see comments]. Science 289 (2000) 739-745
68. Parnot C., Miserey-Lenkei S., Bardin S., Corvol P., and Clauser E. Lessons from constitutively active mutants of G protein-coupled receptors. Trends Endocrinol. Metab. 13 (2002) 336-343
69. Petaja-Repo U.E., Hogue M., Bhalla S., Laperriere A., Morello J.P., and Bouvier M. Ligands act as pharmacological chaperones and increase the efficiency of delta opioid receptor maturation. EMBO J. 21 (2002) 1628-1637
70. Pin J.P., Galvez T., and Prezeau L. Evolution, structure, and activation mechanism of family 3/c G-protein-coupled receptors. Pharmacol. Ther. 98 (2003) 325-354
71. Pin J.P., Kniazeff J., Goudet C., Bessis A.S., Liu J., Galvez T., Acher F., Rondard P., and Prezeau L. The activation mechanism of class-c G-protein coupled receptors. Biol. Cell 96 (2004) 335-342
72. Rasmussen S.G., Jensen A.D., Liapakis G., Ghanouni P., Javitch J.A., and Gether U. Mutation of a highly conserved aspartic acid in the beta2 adrenergic receptor: Constitutive activation, structural instability, and conformational rearrangement of transmembrane segment 6. Mol. Pharmacol. 56 (1999) 175-184
73. 2+ receptor. J. Biol. Chem. 277 (2002) 18908-18913
74. Ridge K.D., Abdulaev N.G., Sousa M., and Palczewski K. Phototransduction: Crystal clear. Trends Biochem. Sci. 28 (2003) 479-487
75. Ruprecht J.J., Mielke T., Vogel R., Villa C., and Schertler G.F. Electron crystallography reveals the structure of metarhodopsin I. EMBO J. 23 (2004) 3609-3620
76. Sakmar T.P. Structure of rhodopsin and the superfamily of seven-helical receptors: The same and not the same. Curr. Opin. Cell Biol. 14 (2002) 189-195
77. Sakmar T.P., Franke R.R., and Khorana H.G. The role of the retinylidene schiff base counterion in rhodopsin in determining wavelength absorbance and schiff base pKa. Proc. Natl. Acad. Sci. USA 88 (1991) 3079-3083
78. Samama P., Cotecchia S., Costa T., and Lefkowitz R.J. A mutation-induced activated state of the beta 2-adrenergic receptor. Extending the ternary complex model. J. Biol. Chem. 268 (1993) 4625-4636
79. Scheer A., Fanelli F., Costa T., De Benedetti P.G., and Cotecchia S. Constitutively active mutants of the alpha 1b-adrenergic receptor: Role of highly conserved polar amino acids in receptor activation. EMBO J. 15 (1996) 3566-3578
80. Schertler G.F. Structure of rhodopsin and the metarhodopsin I photointermediate. Curr. Opin. Struct. Biol. 15 (2005) 408-415
81. Schertler G.F., Villa C., and Henderson R. Projection structure of rhodopsin. Nature 362 (1993) 770-772
82. Schoneberg T., Liu J., and Wess J. Plasma membrane localization and functional rescue of truncated forms of a G protein-coupled receptor. J. Biol. Chem. 270 (1995) 18000-18006
83. Shapiro D.A., Kristiansen K., Weiner D.M., Kroeze W.K., and Roth B.L. Evidence for a model of agonist-induced activation of 5-hydroxytryptamine 2a serotonin receptors that involves the disruption of a strong ionic interaction between helices 3 and 6. J. Biol. Chem. 277 (2002) 11441-11449
84. Sharma S., and Sharma S.C. An update on eicosanoids and inhibitors of cyclooxygenase enzyme systems. Indian J. Exp. Biol. 35 (1997) 1025-1031
85. Sheikh S.P., Zvyaga T.A., Lichtarge O., Sakmar T.P., and Bourne H.R. Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F. Nature 383 (1996) 347-350
86. Sheikh S.P., Vilardarga J.P., Baranski T.J., Lichtarge O., Iiri T., Meng E.C., Nissenson R.A., and Bourne H.R. Similar structures and shared switch mechanisms of the beta2-adrenoceptor and the parathyroid hormone receptor. Zn(II) bridges between helices III and VI block activation. J. Biol. Chem. 274 (1999) 17033-17041
87. Shi L., Liapakis G., Xu R., Guarnieri F., Ballesteros J.A., and Javitch J.A. Beta2 adrenergic receptor activation. Modulation of the proline kink in transmembrane 6 by a rotamer toggle switch. J. Biol. Chem. 277 (2002) 40989-40996
88. Sprang S.R. G protein mechanisms: Insights from structural analysis. Annu. Rev. Biochem. 66 (1997) 639-678
89. Strader C.D., Candelore M.R., Hill W.S., Dixon R.A., and Sigal I.S. A single amino acid substitution in the beta-adrenergic receptor promotes partial agonist activity from antagonists. J. Biol. Chem. 264 (1989) 16470-16477
90. Strader C.D., Candelore M.R., Hill W.S., Sigal I.S., and Dixon R.A. Identification of two serine residues involved in agonist activation of the beta-adrenergic receptor. J. Biol. Chem. 264 (1989) 13572-13578
91. Strader C.D., Sigal I.S., and Dixon R.A. Structural basis of beta-adrenergic receptor function. FASEB J. 3 (1989) 1825-1832
92. Swaminath G., Xiang Y., Lee T.W., Steenhuis J., Parnot C., and Kobilka B.K. Sequential binding of agonists to the {beta}2 adrenoceptor: Kinetic evidence for intermediate conformational states. J. Biol. Chem. 279 (2004) 686-691
93. Swaminath G., Deupi X., Lee T.W., Zhu W., Thian F.S., Kobilka T.S., and Kobilka B. Probing the beta2 adrenoceptor binding site with catechol reveals differences in binding and activation by agonists and partial agonists. J. Biol. Chem. 280 (2005) 22165-22171
94. Tateyama M., Abe H., Nakata H., Saito O., and Kubo Y. Ligand-induced rearrangement of the dimeric metabotropic glutamate receptor 1alpha. Nat. Struct. Mol. Biol. 11 (2004) 637-642
95. Teller D.C., Okada T., Behnke C.A., Palczewski K., and Stenkamp R.E. Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs). Biochemistry 40 (2001) 7761-7772
96. Tsuchiya D., Kunishima N., Kamiya N., Jingami H., and Morikawa K. Structural views of the ligand-binding cores of a metabotropic glutamate receptor complexed with an antagonist and both glutamate and Gd3+. Proc. Natl. Acad. Sci. USA 99 (2002) 2660-2665
97. Ward S.D., Hamdan F.F., Bloodworth L.M., and Wess J. Conformational changes that occur during M3 muscarinic acetylcholine receptor activation probed by the use of an in situ disulfide cross-linking strategy. J. Biol. Chem. 277 (2002) 2247-2257
98. Wei H., Ahn S., Shenoy S.K., Karnik S.S., Hunyady L., Luttrell L.M., and Lefkowitz R.J. Independent beta-arrestin 2 and G protein-mediated pathways for angiotensin II activation of extracellular signal-regulated kinases 1 and 2. Proc. Natl. Acad. Sci. USA 100 (2003) 10782-10787
99. Weiss J.M., Morgan P.H., Lutz M.W., and Kenakin T.P. The cubic ternary complex receptor-occupancy model. III. Resurrecting efficacy. J. Theor. Biol. 181 (1996) 381-397
100. Wieland K., Zuurmond H.M., Krasel C., Ijzerman A.P., and Lohse M.J. Involvement of Asn-293 in stereospecific agonist recognition and in activation of the beta 2-adrenergic receptor. Proc. Natl. Acad. Sci. USA 93 (1996) 9276-9281
101. Wilson A.L., Guyer C.A., Cragoe E.J., and Limbird L.E. The hydrophobic tryptic core of the porcine alpha 2-adrenergic receptor retains allosteric modulation of binding by Na+, H+, and 5-amino-substituted amiloride analogs. J. Biol. Chem. 265 (1990) 17318-17322
102. Yi C.S., Song Y.S., Ryu K.S., Sohn J., Ji I., and Ji T.H. Common and differential mechanisms of gonadotropin receptors. Cell. Mol. Life Sci. 59 (2002) 932-940