Crossref
journal-article
Springer Science and Business Media LLC
Nature (297)
References
70
Referenced
2,054
-
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). This paper provides a comprehensive analysis of sequence relationships between G-protein-coupled receptors in the human genome.
(
10.1124/mol.63.6.1256
) / Mol. Pharmacol. by R Fredriksson (2003) -
Hoffman, B. B. & Lefkowitz, R. J. Adrenergic receptors in the heart. Annu. Rev. Physiol. 44, 475–484 (1982).
(
10.1146/annurev.ph.44.030182.002355
) / Annu. Rev. Physiol. by BB Hoffman (1982) -
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).
(
10.1016/S0026-895X(25)10009-6
) / Mol. Pharmacol. by P Samama (1994) -
Chidiac, P., Hebert, T. E., Valiquette, M., Dennis, M. & Bouvier, M. Inverse agonist activity of beta-adrenergic antagonists. Mol. Pharmacol. 45, 490–499 (1994).
(
10.1016/S0026-895X(25)10022-9
) / Mol. Pharmacol. by P Chidiac (1994) -
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).
(
10.1161/01.RES.85.11.1092
) / Circ. Res. by RP Xiao (1999) -
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).
(
10.1074/jbc.M506576200
) / J. Biol. Chem. by SK Shenoy (2006) -
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).
(
10.1073/pnas.1936664100
) / Proc. Natl Acad. Sci. USA by M Azzi (2003) - Freedman, N. J. & Lefkowitz, R. J. Desensitization of G protein-coupled receptors. Recent Prog. Horm. Res. 51, 319–351; discussion 352–353 (1996). / Recent Prog. Horm. Res. by NJ Freedman (1996)
-
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).
(
10.1146/annurev.pharmtox.48.113006.094830
) / Annu. Rev. Pharmacol. Toxicol. by AC Hanyaloglu (2008) -
Terrillon, S. & Bouvier, M. Roles of G-protein-coupled receptor dimerization. EMBO Rep. 5, 30–34 (2004).
(
10.1038/sj.embor.7400052
) / EMBO Rep. by S Terrillon (2004) -
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).
(
10.1196/annals.1341.015
) / Ann. NY Acad. Sci. by PA Insel (2005) -
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).
(
10.1073/pnas.101126198
) / Proc. Natl Acad. Sci. USA by P Ghanouni (2001) -
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).
(
10.1074/jbc.M310888200
) / J. Biol. Chem. by G Swaminath (2004) -
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).
(
10.1074/jbc.M502352200
) / J. Biol. Chem. by G Swaminath (2005) -
Galandrin, S., Oligny-Longpre, G. & Bouvier, M. The evasive nature of drug efficacy: implications for drug discovery. Trends Pharmacol. Sci. 28, 423–430 (2007).
(
10.1016/j.tips.2007.06.005
) / Trends Pharmacol. Sci. by S Galandrin (2007) -
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).
(
10.1073/pnas.0707936104
) / Proc. Natl Acad. Sci. USA by JW Wisler (2007) -
Kobilka, B. K. & Deupi, X. Conformational complexity of G-protein-coupled receptors. Trends Pharmacol. Sci. 28, 397–406 (2007).
(
10.1016/j.tips.2007.06.003
) / Trends Pharmacol. Sci. by BK Kobilka (2007) -
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).
(
10.1006/jmbi.1998.2070
) / J. Mol. Biol. by A Krebs (1998) -
Schertler, G. F., Villa, C. & Henderson, R. Projection structure of rhodopsin. Nature 362, 770–772 (1993). This paper presents the first three-dimensional structure of a G-protein-coupled receptor using cryoelectron microscopy of two-dimensional crystals.
(
10.1038/362770a0
) / Nature by GF Schertler (1993) -
Rasmussen, S. G. et al. Crystal structure of the human β2 adrenergic G-protein-coupled receptor. Nature 450, 383–387 (2007). This is the first reported three-dimensional crystal structure of a ligand-activated G-protein-coupled receptor.
(
10.1038/nature06325
) / Nature by SG Rasmussen (2007) -
Rosenbaum, D. M. et al. GPCR engineering yields high-resolution structural insights into β2-adrenergic receptor function. Science 318, 1266–1273 (2007).
(
10.1126/science.1150609
) / Science by DM Rosenbaum (2007) -
Cherezov, V. et al. High-resolution crystal structure of an engineered human β2-adrenergic G-protein-coupled receptor. Science 318, 1258–1265 (2007).
(
10.1126/science.1150577
) / Science by V Cherezov (2007) -
Hanson, M. A. et al. A specific cholesterol binding site is established by the 2.8 Å structure of the human β2-adrenergic receptor. Structure 16, 897–905 (2008).
(
10.1016/j.str.2008.05.001
) / Structure by MA Hanson (2008) -
Warne, T. et al. Structure of a β1-adrenergic G-protein-coupled receptor. Nature 454, 486–491 (2008).
(
10.1038/nature07101
) / Nature by T Warne (2008) -
Jaakola, V. P. et al. The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist. Science 322, 1211–1217 (2008).
(
10.1126/science.1164772
) / Science by VP Jaakola (2008) -
Palczewski, K. et al. Crystal structure of rhodopsin: A G-protein-coupled receptor. Science 289, 739–745 (2000). This paper presents the first three-dimensional crystal structure of a G-protein-coupled receptor, the visual photoreceptor rhodopsin.
(
10.1126/science.289.5480.739
) / Science by K Palczewski (2000) -
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).
(
10.1016/j.jmb.2004.07.044
) / J. Mol. Biol. by T Okada (2004) -
Li, J., Edwards, P. C., Burghammer, M., Villa, C. & Schertler, G. F. Structure of bovine rhodopsin in a trigonal crystal form. J. Mol. Biol. 343, 1409–1438 (2004).
(
10.1016/j.jmb.2004.08.090
) / J. Mol. Biol. by J Li (2004) -
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).
(
10.1016/S1043-9471(05)80049-7
) / Methods Neurosci. by JA Ballesteros (1995) -
Shi, L. et al. β2 adrenergic receptor activation. Modulation of the proline kink in transmembrane 6 by a rotamer toggle switch. J. Biol. Chem. 277, 40989–40996 (2002).
(
10.1074/jbc.M206801200
) / J. Biol. Chem. by L Shi (2002) -
Horn, F. et al. GPCRDB information system for G protein-coupled receptors. Nucleic Acids Res. 31, 294–297 (2003).
(
10.1093/nar/gkg103
) / Nucleic Acids Res. by F Horn (2003) -
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).
(
10.1038/nrd2760
) / Nature Rev. Drug Discov. by PJ Conn (2009) -
Baker, J. G. The selectivity of β-adrenoceptor antagonists at the human β1, β2 and β3 adrenoceptors. Br. J. Pharmacol. 144, 317–322 (2005).
(
10.1038/sj.bjp.0706048
) / Br. J. Pharmacol. by JG Baker (2005) -
Sugimoto, Y. et al. β1-selective agonist (-)-1-(3,4-dimethoxyphenetylamino)-3-(3,4-dihydroxy)-2-propanol [(-)-RO363] differentially interacts with key amino acids responsible for β1-selective binding in resting and active states. J. Pharmacol. Exp. Ther. 301, 51–58 (2002).
(
10.1124/jpet.301.1.51
) / J. Pharmacol. Exp. Ther. by Y Sugimoto (2002) -
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).
(
10.1016/j.jmb.2008.05.022
) / J. Mol. Biol. by R Vogel (2008) -
Ballesteros, J. A. et al. Activation of the β2-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).
(
10.1074/jbc.M103747200
) / J. Biol. Chem. by JA Ballesteros (2001) -
Rasmussen, S. G. et al. Mutation of a highly conserved aspartic acid in the β2 adrenergic receptor: constitutive activation, structural instability, and conformational rearrangement of transmembrane segment 6. Mol. Pharmacol. 56, 175–184 (1999).
(
10.1124/mol.56.1.175
) / Mol. Pharmacol. by SG Rasmussen (1999) -
Yao, X. et al. Coupling ligand structure to specific conformational switches in the β2-adrenoceptor. Nature Chem. Biol. 2, 417–422 (2006).
(
10.1038/nchembio801
) / Nature Chem. Biol. by X Yao (2006) -
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).
(
10.1016/j.tips.2005.12.007
) / Trends Pharmacol. Sci. by RA Bond (2006) -
Barak, L. S., Menard, L., Ferguson, S. S., Colapietro, A. M. & Caron, M. G. The conserved seven-transmembrane sequence NP(X)2,3Y of the G-protein-coupled receptor superfamily regulates multiple properties of the β2-adrenergic receptor. Biochemistry 34, 15407–15414 (1995).
(
10.1021/bi00047a003
) / Biochemistry by LS Barak (1995) -
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).
(
10.1073/pnas.082666399
) / Proc. Natl Acad. Sci. USA by T Okada (2002) -
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).
(
10.1002/cbic.200600429
) / ChemBioChem by L Pardo (2007) -
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). This paper reports the cloning of the first ligand-activated G-protein-coupled receptor.
(
10.1038/321075a0
) / Nature by RA Dixon (1986) -
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).
(
10.1038/nature07063
) / Nature by JH Park (2008) -
Scheerer, P. et al. Crystal structure of opsin in its G-protein-interacting conformation. Nature 455, 497–502 (2008). This paper presents the high-resolution stucture of an active-state G-protein-coupled receptor in complex with a G-protein peptide.
(
10.1038/nature07330
) / Nature by P Scheerer (2008) -
Lamb, T. D. & Pugh, E. N. Jr. Dark adaptation and the retinoid cycle of vision. Prog. Retin. Eye Res. 23, 307–380 (2004).
(
10.1016/j.preteyeres.2004.03.001
) / Prog. Retin. Eye Res. by TD Lamb (2004) -
Vogel, R. & Siebert, F. Conformations of the active and inactive states of opsin. J. Biol. Chem. 276, 38487–38493 (2001).
(
10.1074/jbc.M105423200
) / J. Biol. Chem. by R Vogel (2001) -
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).
(
10.1021/bi00165a008
) / Biochemistry by GB Cohen (1992) -
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).
(
10.1038/nsmb.1549
) / Nature Struct. Mol. Biol. by S Ahuja (2009) -
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). This is the first biophysical study to demonstrate movement of transmembrane segment 6 upon activation of rhodopsin.
(
10.1126/science.274.5288.768
) / Science by DL Farrens (1996) -
Altenbach, C., Kusnetzow, A. K., Ernst, O. P., Hofmann, K. P. & Hubbell, W. L. High-resolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation. Proc. Natl Acad. Sci. USA 105, 7439–7444 (2008).
(
10.1073/pnas.0802515105
) / Proc. Natl Acad. Sci. USA by C Altenbach (2008) -
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).
(
10.1016/S0021-9258(18)80035-7
) / J. Biol. Chem. by CD Strader (1989) -
Liapakis, G. et al. The forgotten serine. A critical role for Ser-2035.42 in ligand binding to and activation of the β2-adrenergic receptor. J. Biol. Chem. 275, 37779–37788 (2000).
(
10.1074/jbc.M002092200
) / J. Biol. Chem. by G Liapakis (2000) -
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).
(
10.1016/S0021-9258(19)81509-0
) / J. Biol. Chem. by CD Strader (1988) -
Jiang, Q., Lee, B. X., Glashofer, M., van Rhee, A. M. & Jacobson, K. A. Mutagenesis reveals structure-activity parallels between human A2A adenosine receptors and biogenic amine G protein-coupled receptors. J. Med. Chem. 40, 2588–2595 (1997).
(
10.1021/jm970084v
) / J. Med. Chem. by Q Jiang (1997) -
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).
(
10.2174/092986706777442002
) / Curr. Med. Chem. by A Patny (2006) -
Kolb, P. et al. Structure-based discovery of β2-adrenergic receptor ligands. Proc. Natl Acad. Sci. USA 106, 6843–6848 (2009).
(
10.1073/pnas.0812657106
) / Proc. Natl Acad. Sci. USA by P Kolb (2009) -
Ghanouni, P. et al. Functionally different agonists induce distinct conformations in the G protein coupling domain of the β2 adrenergic receptor. J. Biol. Chem. 276, 24433–24436 (2001).
(
10.1074/jbc.C100162200
) / J. Biol. Chem. by P Ghanouni (2001) -
Salom, D. et al. Crystal structure of a photoactivated deprotonated intermediate of rhodopsin. Proc. Natl Acad. Sci. USA 103, 16123–16128 (2006).
(
10.1073/pnas.0608022103
) / Proc. Natl Acad. Sci. USA by D Salom (2006) -
Knierim, B., Hofmann, K. P., Ernst, O. P. & Hubbell, W. L. Sequence of late molecular events in the activation of rhodopsin. Proc. Natl Acad. Sci. USA 104, 20290–20295 (2007).
(
10.1073/pnas.0710393104
) / Proc. Natl Acad. Sci. USA by B Knierim (2007) -
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).
(
10.1016/S0021-9258(20)79672-9
) / J. Biol. Chem. by A De Lean (1980) -
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).
(
10.1016/S0065-3233(03)63010-X
) / Adv. Protein Chem. by WL Hubbell (2003) -
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).
(
10.1007/s10858-007-9205-3
) / J. Biomol. NMR by K Werner (2008) -
Standfuss, J. et al. Crystal structure of a thermally stable rhodopsin mutant. J. Mol. Biol. 372, 1179–1188 (2007).
(
10.1016/j.jmb.2007.03.007
) / J. Mol. Biol. by J Standfuss (2007) -
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).
(
10.1006/jsbi.1999.4209
) / J. Struct. Biol. by T Okada (2000) -
Serrano-Vega, M. J., Magnani, F., Shibata, Y. & Tate, C. G. Conformational thermostabilization of the β1-adrenergic receptor in a detergent-resistant form. Proc. Natl Acad. Sci. USA 105, 877–882 (2008).
(
10.1073/pnas.0711253105
) / Proc. Natl Acad. Sci. USA by MJ Serrano-Vega (2008) -
Day, P. W. et al. A monoclonal antibody for G protein-coupled receptor crystallography. Nature Methods 4, 927–929 (2007).
(
10.1038/nmeth1112
) / Nature Methods by PW Day (2007) -
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).
(
10.1006/jmbi.2001.5295
) / J. Mol. Biol. by S Faham (2002) -
Faham, S. et al. Crystallization of bacteriorhodopsin from bicelle formulations at room temperature. Protein Sci. 14, 836–840 (2005).
(
10.1110/ps.041167605
) / Protein Sci. by S Faham (2005) -
Caffrey, M. Crystallizing membrane proteins for structure determination: use of lipidic mesophases. Annu. Rev. Biophys. 38, doi:10.1146/annurev.biophys.050708.133655 (2008).
(
10.1146/annurev.biophys.050708.133655
)
Dates
Type | When |
---|---|
Created | 16 years, 3 months ago (May 20, 2009, 11:28 a.m.) |
Deposited | 6 months, 2 weeks ago (Feb. 9, 2025, 11:18 a.m.) |
Indexed | 46 minutes ago (Aug. 29, 2025, 2:06 p.m.) |
Issued | 16 years, 3 months ago (May 1, 2009) |
Published | 16 years, 3 months ago (May 1, 2009) |
Published Online | 16 years, 3 months ago (May 20, 2009) |
Published Print | 16 years, 3 months ago (May 1, 2009) |
@article{Rosenbaum_2009, title={The structure and function of G-protein-coupled receptors}, volume={459}, ISSN={1476-4687}, url={http://dx.doi.org/10.1038/nature08144}, DOI={10.1038/nature08144}, number={7245}, journal={Nature}, publisher={Springer Science and Business Media LLC}, author={Rosenbaum, Daniel M. and Rasmussen, Søren G. F. and Kobilka, Brian K.}, year={2009}, month=may, pages={356–363} }