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Volumn 459, Issue 7245, 2009, Pages 356-363

The structure and function of G-protein-coupled receptors

Author keywords

[No Author keywords available]

Indexed keywords

11 CIS RETINAL; ADENOSINE A2 RECEPTOR; ADENOSINE RECEPTOR BLOCKING AGENT; ADRENALIN; BETA 1 ADRENERGIC RECEPTOR; BETA 2 ADRENERGIC RECEPTOR; CARAZOLOL; CENTRAL STIMULANT AGENT; CYANOPINDOLOL; CYCLIC AMP; G PROTEIN COUPLED RECEPTOR; GLUTAMIC ACID; HORMONE; LYSINE; MEMBRANE PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; NEUROTRANSMITTER; NORADRENALIN; PROLINE; RETINA S ANTIGEN; RHODOPSIN; SCHIFF BASE; TIMOLOL; TYROSINE;

EID: 66249144426     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature08144     Document Type: Review
Times cited : (1904)

References (70)
  • 1
    • 0038024615 scopus 로고    scopus 로고
    • The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints
    • Fredriksson, R., Lagerstrom, M. C., Lundin, L. G. & 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, 1256-1272 (2003).
    • (2003) Mol. Pharmacol , vol.63 , pp. 1256-1272
    • Fredriksson, R.1    Lagerstrom, M.C.2    Lundin, L.G.3    Schioth, H.B.4
  • 3
    • 0028209348 scopus 로고
    • Negative antagonists promote an inactive conformation of the beta 2-adrenergic receptor
    • Samama, P., Pei, G., Costa, T., Cotecchia, S. & Lefkowitz, R. J. Negative antagonists promote an inactive conformation of the beta 2-adrenergic receptor. Mol. Pharmacol. 45, 390-394 (1994).
    • (1994) Mol. Pharmacol , vol.45 , pp. 390-394
    • Samama, P.1    Pei, G.2    Costa, T.3    Cotecchia, S.4    Lefkowitz, R.J.5
  • 5
    • 0033607558 scopus 로고    scopus 로고
    • Recent advances in cardiac beta(2)-adrenergic signal transduction
    • Xiao, R. P., Cheng, H., Zhou, Y. Y., Kuschel, M. & Lakatta, E. G. Recent advances in cardiac beta(2)-adrenergic signal transduction. Circ. Res. 85, 1092-1100 (1999).
    • (1999) Circ. Res , vol.85 , pp. 1092-1100
    • Xiao, R.P.1    Cheng, H.2    Zhou, Y.Y.3    Kuschel, M.4    Lakatta, E.G.5
  • 6
    • 33644857279 scopus 로고    scopus 로고
    • Beta-arrestin-dependent, G protein-independent ERK1/2 activation by the beta2 adrenergic receptor
    • Shenoy, S. K. et al. Beta-arrestin-dependent, G protein-independent ERK1/2 activation by the beta2 adrenergic receptor. J. Biol. Chem. 281, 1261-1273 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 1261-1273
    • Shenoy, S.K.1
  • 7
    • 0141593597 scopus 로고    scopus 로고
    • Beta-arrestin-mediated activation of MAPK by inverse agonists reveals distinct active conformations for G protein-coupled receptors
    • Azzi, M. et al. Beta-arrestin-mediated activation of MAPK by inverse agonists reveals distinct active conformations for G protein-coupled receptors. Proc. Natl Acad. Sci. USA 100, 11406-11411 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 11406-11411
    • Azzi, M.1
  • 8
    • 0029719789 scopus 로고    scopus 로고
    • Desensitization of G protein-coupled receptors
    • discussion 352-353
    • Freedman, N. J. & Lefkowitz, R. J. Desensitization of G protein-coupled receptors. Recent Prog. Horm. Res. 51, 319-351; discussion 352-353 (1996).
    • (1996) Recent Prog. Horm. Res , vol.51 , pp. 319-351
    • Freedman, N.J.1    Lefkowitz, R.J.2
  • 9
    • 41149090339 scopus 로고    scopus 로고
    • Regulation of GPCRs by endocytic membrane trafficking and its potential implications
    • Hanyaloglu, A. C. & von Zastrow, M. Regulation of GPCRs by endocytic membrane trafficking and its potential implications. Annu. Rev. Pharmacol. Toxicol. 48, 537-568 (2008).
    • (2008) Annu. Rev. Pharmacol. Toxicol , vol.48 , pp. 537-568
    • Hanyaloglu, A.C.1    von Zastrow, M.2
  • 10
    • 1242276192 scopus 로고    scopus 로고
    • Roles of G-protein-coupled receptor dimerization
    • 30-34
    • Terrillon, S. & Bouvier, M. Roles of G-protein-coupled receptor dimerization. EMBO Rep. 5, 30-34 (2004).
    • (2004) EMBO Rep , vol.5
    • Terrillon, S.1    Bouvier, M.2
  • 11
    • 23744497054 scopus 로고    scopus 로고
    • Caveolae and lipid rafts: G protein-coupled receptor signaling microdomains in cardiac myocytes
    • Insel, P. A. et al. Caveolae and lipid rafts: G protein-coupled receptor signaling microdomains in cardiac myocytes. Ann. NY Acad. Sci. 1047, 166-172 (2005).
    • (2005) Ann. NY Acad. Sci , vol.1047 , pp. 166-172
    • Insel, P.A.1
  • 12
    • 0035932989 scopus 로고    scopus 로고
    • Agonist-induced conformational changes in the G-protein-coupling domain of the beta 2 adrenergic receptor
    • Ghanouni, P., Steenhuis, J. J., Farrens, D. L. & 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, 5997-6002 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 5997-6002
    • Ghanouni, P.1    Steenhuis, J.J.2    Farrens, D.L.3    Kobilka, B.K.4
  • 13
    • 0345791508 scopus 로고    scopus 로고
    • Sequential binding of agonists to the beta2 adrenoceptor. Kinetic evidence for intermediate conformational states
    • Swaminath, G. et al. Sequential binding of agonists to the beta2 adrenoceptor. Kinetic evidence for intermediate conformational states. J. Biol. Chem. 279, 686-691 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 686-691
    • Swaminath, G.1
  • 14
    • 20444499405 scopus 로고    scopus 로고
    • Probing the beta2 adrenoceptor binding site with catechol reveals differences in binding and activation by agonists and partial agonists
    • Swaminath, G. et al. Probing the beta2 adrenoceptor binding site with catechol reveals differences in binding and activation by agonists and partial agonists. J. Biol. Chem. 280, 22165-22171 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 22165-22171
    • Swaminath, G.1
  • 15
    • 34447642715 scopus 로고    scopus 로고
    • The evasive nature of drug efficacy: Implications for drug discovery
    • Galandrin, S., Oligny-Longpre, G. & Bouvier, M. The evasive nature of drug efficacy: implications for drug discovery. Trends Pharmacol. Sci. 28, 423-430 (2007).
    • (2007) Trends Pharmacol. Sci , vol.28 , pp. 423-430
    • Galandrin, S.1    Oligny-Longpre, G.2    Bouvier, M.3
  • 16
    • 36749094552 scopus 로고    scopus 로고
    • A unique mechanism of beta-blocker action: Carvedilol stimulates beta-arrestin signaling
    • Wisler, J. W. et al. A unique mechanism of beta-blocker action: carvedilol stimulates beta-arrestin signaling. Proc. Natl Acad. Sci. USA 104, 16657-16662 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 16657-16662
    • Wisler, J.W.1
  • 17
    • 34447633368 scopus 로고    scopus 로고
    • Conformational complexity of G-protein-coupled receptors
    • Kobilka, B. K. & Deupi, X. Conformational complexity of G-protein-coupled receptors. Trends Pharmacol. Sci. 28, 397-406 (2007).
    • (2007) Trends Pharmacol. Sci , vol.28 , pp. 397-406
    • Kobilka, B.K.1    Deupi, X.2
  • 18
    • 0032500697 scopus 로고    scopus 로고
    • Characterisation of an improved two-dimensional p22121 crystal from bovine rhodopsin
    • Krebs, A., Villa, C., Edwards, P. C. & Schertler, G. F. Characterisation of an improved two-dimensional p22121 crystal from bovine rhodopsin. J. Mol. Biol. 282, 991-1003 (1998).
    • (1998) J. Mol. Biol , vol.282 , pp. 991-1003
    • Krebs, A.1    Villa, C.2    Edwards, P.C.3    Schertler, G.F.4
  • 19
    • 0027190359 scopus 로고
    • Projection structure of rhodopsin
    • Schertler, G. F., Villa, C. & Henderson, R. Projection structure of rhodopsin. Nature 362, 770-772 (1993).
    • (1993) Nature , vol.362 , pp. 770-772
    • Schertler, G.F.1    Villa, C.2    Henderson, R.3
  • 20
    • 36248970132 scopus 로고    scopus 로고
    • 2 adrenergic G-protein-coupled receptor
    • 2 adrenergic G-protein-coupled receptor. Nature 450, 383-387 (2007).
    • (2007) Nature , vol.450 , pp. 383-387
    • Rasmussen, S.G.1
  • 21
    • 36448978229 scopus 로고    scopus 로고
    • 2-adrenergic receptor function
    • 2-adrenergic receptor function. Science 318, 1266-1273 (2007).
    • (2007) Science , vol.318 , pp. 1266-1273
    • Rosenbaum, D.M.1
  • 22
    • 36448995359 scopus 로고    scopus 로고
    • 2-adrenergic G-protein-coupled receptor
    • 2-adrenergic G-protein-coupled receptor. Science 318, 1258-1265 (2007).
    • (2007) Science , vol.318 , pp. 1258-1265
    • Cherezov, V.1
  • 23
    • 44649172481 scopus 로고    scopus 로고
    • 2- adrenergic receptor
    • 2- adrenergic receptor. Structure 16, 897-905 (2008).
    • (2008) Structure , vol.16 , pp. 897-905
    • Hanson, M.A.1
  • 24
    • 47949129742 scopus 로고    scopus 로고
    • 1-adrenergic G-protein-coupled receptor
    • 1-adrenergic G-protein-coupled receptor. Nature 454, 486-491 (2008).
    • (2008) Nature , vol.454 , pp. 486-491
    • Warne, T.1
  • 25
    • 56749103466 scopus 로고    scopus 로고
    • 2A adenosine receptor bound to an antagonist
    • 2A adenosine receptor bound to an antagonist. Science 322, 1211-1217 (2008).
    • (2008) Science , vol.322 , pp. 1211-1217
    • Jaakola, V.P.1
  • 26
    • 0034604451 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: A G-protein-coupled receptor
    • Palczewski, K. et al. Crystal structure of rhodopsin: A G-protein-coupled receptor. Science 289, 739-745 (2000).
    • (2000) Science , vol.289 , pp. 739-745
    • Palczewski, K.1
  • 27
    • 4344581120 scopus 로고    scopus 로고
    • The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure
    • Okada, T. et al. The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure. J. Mol. Biol. 342, 571-583 (2004).
    • (2004) J. Mol. Biol , vol.342 , pp. 571-583
    • Okada, T.1
  • 29
    • 77957055780 scopus 로고
    • Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein coupled receptors
    • Ballesteros, J. A. & Weinstein, H. 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 (1995).
    • (1995) Methods Neurosci , vol.25 , pp. 366-428
    • Ballesteros, J.A.1    Weinstein, H.2
  • 30
    • 0037174606 scopus 로고    scopus 로고
    • 2 adrenergic receptor activation. Modulation of the proline kink in transmembrane 6 by a rotamer toggle switch
    • 2 adrenergic receptor activation. Modulation of the proline kink in transmembrane 6 by a rotamer toggle switch. J. Biol. Chem. 277, 40989-40996 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 40989-40996
    • Shi, L.1
  • 31
    • 0037252680 scopus 로고    scopus 로고
    • GPCRDB information system for G protein-coupled receptors
    • Horn, F. et al. GPCRDB information system for G protein-coupled receptors. Nucleic Acids Res. 31, 294-297 (2003).
    • (2003) Nucleic Acids Res , vol.31 , pp. 294-297
    • Horn, F.1
  • 32
    • 58149193205 scopus 로고    scopus 로고
    • Allosteric modulators of GPCRs: A novel approach for the treatment of CNS disorders
    • Conn, P. J., Christopoulos, A. & Lindsley, C. W. Allosteric modulators of GPCRs: a novel approach for the treatment of CNS disorders. Nature Rev. Drug Discov. 8, 41-54 (2009).
    • (2009) Nature Rev. Drug Discov , vol.8 , pp. 41-54
    • Conn, P.J.1    Christopoulos, A.2    Lindsley, C.W.3
  • 33
    • 14644421602 scopus 로고    scopus 로고
    • The selectivity of β-adrenoceptor antagonists at the human β1, β2 and β3 adrenoceptors
    • Baker, J. G. The selectivity of β-adrenoceptor antagonists at the human β1, β2 and β3 adrenoceptors. Br. J. Pharmacol. 144, 317-322 (2005).
    • (2005) Br. J. Pharmacol , vol.144 , pp. 317-322
    • Baker, J.G.1
  • 34
    • 0036128982 scopus 로고    scopus 로고
    • 1-selective binding in resting and active states
    • 1-selective binding in resting and active states. J. Pharmacol. Exp. Ther. 301, 51-58 (2002).
    • (2002) J. Pharmacol. Exp. Ther , vol.301 , pp. 51-58
    • Sugimoto, Y.1
  • 35
    • 45649083187 scopus 로고    scopus 로고
    • Functional role of the "ionic lock" - an interhelical hydrogen-bond network in family A heptahelical receptors
    • Vogel, R. et al. Functional role of the "ionic lock" - an interhelical hydrogen-bond network in family A heptahelical receptors. J. Mol. Biol. 380, 648-655 (2008).
    • (2008) J. Mol. Biol , vol.380 , pp. 648-655
    • Vogel, R.1
  • 36
    • 0035800850 scopus 로고    scopus 로고
    • 2- adrenergic receptor involves disruption of an ionic lock between the cytoplasmic ends of transmembrane segments 3 and 6
    • 2- adrenergic receptor involves disruption of an ionic lock between the cytoplasmic ends of transmembrane segments 3 and 6. J. Biol. Chem. 276, 29171-29177 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 29171-29177
    • Ballesteros, J.A.1
  • 37
    • 0033061256 scopus 로고    scopus 로고
    • 2 adrenergic receptor: Constitutive activation, structural instability, and conformational rearrangement of transmembrane segment 6
    • 2 adrenergic receptor: constitutive activation, structural instability, and conformational rearrangement of transmembrane segment 6. Mol. Pharmacol. 56, 175-184 (1999).
    • (1999) Mol. Pharmacol , vol.56 , pp. 175-184
    • Rasmussen, S.G.1
  • 38
    • 33746382921 scopus 로고    scopus 로고
    • 2-adrenoceptor. Nature Chem. Biol. 2, 417-422 (2006).
    • 2-adrenoceptor. Nature Chem. Biol. 2, 417-422 (2006).
  • 39
    • 31844446495 scopus 로고    scopus 로고
    • Recent developments in constitutive receptor activity and inverse agonism, and their potential for GPCR drug discovery
    • Bond, R. A. & Ijzerman, A. P. Recent developments in constitutive receptor activity and inverse agonism, and their potential for GPCR drug discovery. Trends Pharmacol. Sci. 27, 92-96 (2006).
    • (2006) Trends Pharmacol. Sci , vol.27 , pp. 92-96
    • Bond, R.A.1    Ijzerman, A.P.2
  • 41
    • 0037197848 scopus 로고    scopus 로고
    • Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography
    • Okada, T. et al. Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography. Proc. Natl Acad. Sci. USA 99, 5982-5987 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 5982-5987
    • Okada, T.1
  • 42
    • 33846302070 scopus 로고    scopus 로고
    • The role of internal water molecules in the structure and function of the rhodopsin family of G protein-coupled receptors
    • Pardo, L., Deupi, X., Dolker, N., Lopez-Rodriguez, M. L. & Campillo, M. The role of internal water molecules in the structure and function of the rhodopsin family of G protein-coupled receptors. ChemBioChem 8, 19-24 (2007).
    • (2007) ChemBioChem , vol.8 , pp. 19-24
    • Pardo, L.1    Deupi, X.2    Dolker, N.3    Lopez-Rodriguez, M.L.4    Campillo, M.5
  • 43
    • 0022485749 scopus 로고
    • Cloning of the gene and cDNA for mammalian β-adrenergic receptor and homology with rhodopsin
    • Dixon, R. A. et al. Cloning of the gene and cDNA for mammalian β-adrenergic receptor and homology with rhodopsin. Nature 321, 75-79 (1986).
    • (1986) Nature , vol.321 , pp. 75-79
    • Dixon, R.A.1
  • 44
    • 47049130668 scopus 로고    scopus 로고
    • Crystal structure of the ligand-free G-protein-coupled receptor opsin
    • Park, J. H., Scheerer, P., Hofmann, K. P., Choe, H. W. & Ernst, O. P. Crystal structure of the ligand-free G-protein-coupled receptor opsin. Nature 454 183-187 (2008).
    • (2008) Nature , vol.454 , pp. 183-187
    • Park, J.H.1    Scheerer, P.2    Hofmann, K.P.3    Choe, H.W.4    Ernst, O.P.5
  • 45
    • 52949102889 scopus 로고    scopus 로고
    • Crystal structure of opsin in its G-protein-interacting conformation
    • Scheerer, P. et al. Crystal structure of opsin in its G-protein-interacting conformation. Nature 455, 497-502 (2008).
    • (2008) Nature , vol.455 , pp. 497-502
    • Scheerer, P.1
  • 46
    • 2942617209 scopus 로고    scopus 로고
    • Dark adaptation and the retinoid cycle of vision
    • Lamb, T. D. & Pugh, E. N. Jr. Dark adaptation and the retinoid cycle of vision. Prog. Retin. Eye Res. 23, 307-380 (2004).
    • (2004) Prog. Retin. Eye Res , vol.23 , pp. 307-380
    • Lamb, T.D.1    Pugh Jr., E.N.2
  • 47
    • 0035914463 scopus 로고    scopus 로고
    • Conformations of the active and inactive states of opsin
    • Vogel, R. & Siebert, F. Conformations of the active and inactive states of opsin. J. Biol. Chem. 276, 38487-38493 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 38487-38493
    • Vogel, R.1    Siebert, F.2
  • 48
    • 0027050784 scopus 로고
    • Mechanism of activation and inactivation of opsin: Role of Glu113 and Lys296
    • Cohen, G. B., Oprian, D. D. & Robinson, P. R. Mechanism of activation and inactivation of opsin: role of Glu113 and Lys296. Biochemistry 31, 12592-12601 (1992).
    • (1992) Biochemistry , vol.31 , pp. 12592-12601
    • Cohen, G.B.1    Oprian, D.D.2    Robinson, P.R.3
  • 49
    • 59649112109 scopus 로고    scopus 로고
    • Helix movement is coupled to displacement of the second extracellular loop in rhodopsin activation
    • Ahuja, S. et al. Helix movement is coupled to displacement of the second extracellular loop in rhodopsin activation. Nature Struct. Mol. Biol. 16, 168-175 (2009).
    • (2009) Nature Struct. Mol. Biol , vol.16 , pp. 168-175
    • Ahuja, S.1
  • 50
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • 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).
    • (1996) Science , vol.274 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 51
    • 44949236117 scopus 로고    scopus 로고
    • Highresolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation
    • Altenbach, C., Kusnetzow, A. K., Ernst, O. P., Hofmann, K. P. & Hubbell, W. L. Highresolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation. Proc. Natl Acad. Sci. USA 105, 7439-7444 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 7439-7444
    • Altenbach, C.1    Kusnetzow, A.K.2    Ernst, O.P.3    Hofmann, K.P.4    Hubbell, W.L.5
  • 52
    • 0024344941 scopus 로고
    • Identification of two serine residues involved in agonist activation of the β-adrenergic receptor
    • Strader, C. D., Candelore, M. R., Hill, W. S., Sigal, I. S. & Dixon, R. A. Identification of two serine residues involved in agonist activation of the β-adrenergic receptor. J. Biol. Chem. 264, 13572-13578 (1989).
    • (1989) J. Biol. Chem , vol.264 , pp. 13572-13578
    • Strader, C.D.1    Candelore, M.R.2    Hill, W.S.3    Sigal, I.S.4    Dixon, R.A.5
  • 53
    • 0034529234 scopus 로고    scopus 로고
    • 2- adrenergic receptor
    • 2- adrenergic receptor. J. Biol. Chem. 275, 37779-37788 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 37779-37788
    • Liapakis, G.1
  • 54
    • 0023740863 scopus 로고
    • Conserved aspartic acid residues 79 and 113 of the β-adrenergic receptor have different roles in receptor function
    • Strader, C. D. et al. Conserved aspartic acid residues 79 and 113 of the β-adrenergic receptor have different roles in receptor function. J. Biol. Chem. 263, 10267-10271 (1988).
    • (1988) J. Biol. Chem , vol.263 , pp. 10267-10271
    • Strader, C.D.1
  • 56
    • 33744761830 scopus 로고    scopus 로고
    • Homology modeling of G-protein-coupled receptors and implications in drug design
    • Patny, A., Desai, P. V. & Avery, M. A. Homology modeling of G-protein-coupled receptors and implications in drug design. Curr. Med. Chem. 13, 1667-1691 (2006).
    • (2006) Curr. Med. Chem , vol.13 , pp. 1667-1691
    • Patny, A.1    Desai, P.V.2    Avery, M.A.3
  • 57
    • 66149149851 scopus 로고    scopus 로고
    • 2- adrenergic receptor ligands
    • 2- adrenergic receptor ligands. Proc. Natl Acad. Sci. USA 106, 6843-6848 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 6843-6848
    • Kolb, P.1
  • 58
    • 0035816704 scopus 로고    scopus 로고
    • 2 adrenergic receptor
    • 2 adrenergic receptor. J. Biol. Chem. 276, 24433-24436 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 24433-24436
    • Ghanouni, P.1
  • 59
    • 33750836895 scopus 로고    scopus 로고
    • Crystal structure of a photoactivated deprotonated intermediate of rhodopsin
    • Salom, D. et al. Crystal structure of a photoactivated deprotonated intermediate of rhodopsin. Proc. Natl Acad. Sci. USA 103, 16123-16128 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 16123-16128
    • Salom, D.1
  • 60
  • 61
    • 0019137579 scopus 로고
    • A ternary complex model explains the agonist-specific binding properties of the adenylate cyclase-coupled β-adrenergic receptor
    • De Lean, A., Stadel, J. M. & Lefkowitz, R. J. A ternary complex model explains the agonist-specific binding properties of the adenylate cyclase-coupled β-adrenergic receptor. J. Biol. Chem. 255, 7108-7117 (1980).
    • (1980) J. Biol. Chem , vol.255 , pp. 7108-7117
    • De Lean, A.1    Stadel, J.M.2    Lefkowitz, R.J.3
  • 62
    • 0037285444 scopus 로고    scopus 로고
    • Rhodopsin structure, dynamics, and activation: A perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking
    • Hubbell, W. L., Altenbach, C., Hubbell, C. M. & 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, 243-290 (2003).
    • (2003) Adv. Protein Chem , vol.63 , pp. 243-290
    • Hubbell, W.L.1    Altenbach, C.2    Hubbell, C.M.3    Khorana, H.G.4
  • 63
    • 37849009111 scopus 로고    scopus 로고
    • Isotope labeling of mammalian GPCRs in HEK293 cells and characterization of the C-terminus of bovine rhodopsin by high resolution liquid NMR spectroscopy
    • Werner, K., Richter, C., Klein-Seetharaman, J. & Schwalbe, H. Isotope labeling of mammalian GPCRs in HEK293 cells and characterization of the C-terminus of bovine rhodopsin by high resolution liquid NMR spectroscopy. J. Biomol. NMR 40, 49-53 (2008).
    • (2008) J. Biomol. NMR , vol.40 , pp. 49-53
    • Werner, K.1    Richter, C.2    Klein-Seetharaman, J.3    Schwalbe, H.4
  • 64
    • 34548529916 scopus 로고    scopus 로고
    • Crystal structure of a thermally stable rhodopsin mutant
    • Standfuss, J. et al. Crystal structure of a thermally stable rhodopsin mutant. J. Mol. Biol. 372, 1179-1188 (2007).
    • (2007) J. Mol. Biol , vol.372 , pp. 1179-1188
    • Standfuss, J.1
  • 65
    • 0343081370 scopus 로고    scopus 로고
    • X-ray diffraction analysis of three-dimensional crystals of bovine rhodopsin obtained from mixed micelles
    • Okada, T. et al. X-ray diffraction analysis of three-dimensional crystals of bovine rhodopsin obtained from mixed micelles. J. Struct. Biol. 130, 73-80 (2000).
    • (2000) J. Struct. Biol , vol.130 , pp. 73-80
    • Okada, T.1
  • 67
    • 35748947246 scopus 로고    scopus 로고
    • A monoclonal antibody for G protein-coupled receptor crystallography
    • Day, P. W. et al. A monoclonal antibody for G protein-coupled receptor crystallography. Nature Methods 4, 927-929 (2007).
    • (2007) Nature Methods , vol.4 , pp. 927-929
    • Day, P.W.1
  • 68
    • 0036301007 scopus 로고    scopus 로고
    • Bicelle crystallization: A new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure
    • Faham, S. & Bowie, J. U. Bicelle crystallization: a new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure. J. Mol. Biol. 316, 1-6 (2002).
    • (2002) J. Mol. Biol , vol.316 , pp. 1-6
    • Faham, S.1    Bowie, J.U.2
  • 69
    • 14144250152 scopus 로고    scopus 로고
    • Crystallization of bacteriorhodopsin from bicelle formulations at room temperature
    • Faham, S. et al. Crystallization of bacteriorhodopsin from bicelle formulations at room temperature. Protein Sci. 14, 836-840 (2005).
    • (2005) Protein Sci , vol.14 , pp. 836-840
    • Faham, S.1
  • 70
    • 66049128793 scopus 로고    scopus 로고
    • Crystallizing membrane proteins for structure determination: Use of lipidic mesophases
    • doi:10.1146/annurev.biophys.050708.133655
    • Caffrey, M. Crystallizing membrane proteins for structure determination: use of lipidic mesophases. Annu. Rev. Biophys. 38, doi:10.1146/annurev.biophys.050708.133655 (2008).
    • (2008) Annu. Rev. Biophys , vol.38
    • Caffrey, M.1


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