Structure of a β1-adrenergic G-protein-coupled receptor

Nature

Volumn 454, Issue 7203, 2008, Pages 486-491

  Warne, Tony ^a   Serrano Vega, Maria J ^a   Baker, Jillian G ^b   Moukhametzianov, Rouslan ^a   Edwards, Patricia C ^a   Henderson, Richard ^a   Leslie, Andrew G W ^a   Tate, Christopher G ^a   Schertler, Gebhard F X ^a  

^a MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

^b UNIVERSITY OF NOTTINGHAM   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

3 ISOPROPYLAMINO 1 (7 METHYL 4 INDANYLOXY) 2 BUTANOL; 5 [2 [[2 HYDROXY 3 [4 (1 METHYL 4 TRIFLUOROMETHYL 2 IMIDAZOLYL)PHENOXY]PROPYL]AMINO]ETHOXY]SALICYLAMIDE; ADRENALIN; AMINO ACID; BETA 1 ADRENERGIC RECEPTOR; BETA 2 ADRENERGIC RECEPTOR; CARAZOLOL; CYANOPINDOLOL; DIHYDROALPRENOLOL; G PROTEIN COUPLED RECEPTOR; ISOPRENALINE; NORADRENALIN; RHODOPSIN; SODIUM ION; TYROSINE; BETA ADRENERGIC RECEPTOR BLOCKING AGENT; DRUG DERIVATIVE; LIGAND; MUTANT PROTEIN; PINDOLOL; PROPANOLAMINE DERIVATIVE;

DRUG; GENETIC STRUCTURE; MEMBRANE; PROTEIN;

ALPHA HELIX; ARTICLE; BINDING AFFINITY; CONFORMATION; CRYSTAL STRUCTURE; CRYSTALLIZATION; CYTOPLASM; DISULFIDE BOND; DRUG RECEPTOR BINDING; EXTRACELLULAR SPACE; LIGAND BINDING; MELEAGRIS GALLOPAVO; MUTAGENESIS; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN MOTIF; PROTEIN STRUCTURE; RECEPTOR UPREGULATION; THERMOSTABILITY; TURKEY (BIRD); ANIMAL; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; DRUG ANTAGONISM; DRUG POTENTIATION; GENETICS; METABOLISM; MUTATION; PROTEIN CONFORMATION; THERMODYNAMICS; X RAY CRYSTALLOGRAPHY;

EUKARYOTA; MELEAGRIS GALLOPAVO;

ADRENERGIC BETA-ANTAGONISTS; AMINO ACID MOTIFS; ANIMALS; BINDING SITES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; LIGANDS; MODELS, MOLECULAR; MUTANT PROTEINS; MUTATION; PINDOLOL; PROPANOLAMINES; PROTEIN CONFORMATION; RECEPTORS, ADRENERGIC, BETA-1; THERMODYNAMICS; TURKEYS;

EID: 47949129742     PISSN: 00280836     EISSN: 14764679     Source Type: Journal    
DOI: 10.1038/nature07101     Document Type: Article

References (52)

1. Fredriksson, R. & Schioth, H. B. The repertoire of G-protein-coupled receptors in fully sequenced genomes. Mol. Pharmacol. 67, 1414-1425 (2005).
2. 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).
3. Altenbach, C. et al. High resolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation. Proc. Natl Acad. Sci. USA 105, 7439-7444 (2008).
4. Foord, S. M. et al. International Union of Pharmacology. XLVI. G protein-coupled receptor list. Pharmacol. Rev. 57, 279-288 (2005).
5. Baldwin, J. M., Schertler, G. F. & Unger, V. M. An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors. J. Mol. Biol. 272, 144-164 (1997).
6. Bockaert, J. & Pin, J. P. Molecular tinkering of G protein-coupled receptors: an evolutionary success. EMBO J. 18, 1723-1729 (1999).
7. 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).
8. Black, J. W. Drugs from emasculated hormones - the principle of syntopic antagonism (Nobel lecture). Angew. Chem. Int. Edn Engl. 28, 886-894 (1989).
9. 2 adrenergic G-protein-coupled receptor. Nature 450, 383-387 (2007).
10. 2-adrenergic G protein-coupled receptor. Science 318, 1258-1265 (2007).
11. 3 adrenoceptors. Br. J. Pharmacol. 144, 317-322 (2005).
12. 1-selective binding in resting and active states. J. Pharmacol. Exp. Ther. 301, 51-58 (2002).
13. Gether, U. et al. Structural instability of a constitutively active G protein-coupled receptor. Agonist-independent activation due to conformational flexibility. J. Biol. Chem. 272, 2587-2590 (1997).
14. Parker, E. M., Kameyama, K., Higashijima, T. & Ross, E. M. Reconstitutively active G protein-coupled receptors purified from baculovirus-infected insect cells. J. Biol. Chem. 266, 519-527 (1991).
15. Serrano-Vega, M. J., Magnani, F., Shibata, Y. & Tate, C. G. Conformational thermostabilization of the beta1-adrenergic receptor in a detergent-resistant form. Proc. Natl Acad. Sci. USA 105, 877-882 (2008).
16. 1-adrenoceptor. J. Pharmacol. Exp. Ther. 313, 1163-1171 (2005).
17. 1-adrenergic receptor. FEBS Lett. 457, 302-306 (1999).
18. 2-adrenergic receptor. Mol. Pharmacol. 45, 390-394 (1994).
19. Yarden, Y. et al. The avian β-adrenergic receptor: primary structure and membrane topology. Proc. Natl Acad. Sci. USA 83, 6795-6799 (1986).
20. Harding, M. M. Metal-ligand geometry relevant to proteins and in proteins: sodium and potassium. Acta Crystallogr. D 58, 872-874 (2002).
21. Burstein, E. S., Spalding, T. A. & Brann, M. R. The second intracellular loop of the m5 muscarinic receptor is the switch which enables G-protein coupling. J. Biol. Chem. 273, 24322-24327 (1998).
22. Wong, S. K. F., Parker, E. M. & Ross, E. M. Chimeric muscarinic cholinergic β-adrenergic receptors that activate Gs in response to muscarinic agonists. J. Biol. Chem. 265, 6219-6224 (1990).
23. Wong, S. K. F. & Ross, E. M. Chimeric muscarinic cholinergic:β- adrenergic receptors that are functionally promiscuous among G-proteins. J. Biol. Chem. 269, 18968-18976 (1994).
24. Wess, J., Bonner, T. I., Dorje, F. & Brann, M. R. Delineation of muscarinic receptor domains conferring selectivity of coupling to guanine nucleotide-binding proteins and 2nd messengers. Mol. Pharmacol. 38, 517-523 (1990).
25. Scarselli, M., Li, B., Kim, S. K. & Wess, J. Multiple residues in the second extracellular loop are critical for M3 muscarinic acetylcholine receptor activation. J. Biol. Chem. 282, 7385-7396 (2007).
26. Li, J. et al. Structure of bovine rhodopsin in a trigonal crystal form. J. Mol. Biol. 343, 1409-1438 (2004).
27. 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).
28. Palczewski, K. et al. Crystal structure of rhodopsin: a G protein-coupled receptor. Science 289, 739-745 (2000).
29. Okada, T. et al. The retinal conformation and its environment in rhodopsin in light of a new 2.2 angstrom crystal structure. J. Mol. Biol. 342, 571-583 (2004).
30. 2- selective agonist TA-2005. Mol. Pharmacol. 53, 128-134 (1998).
31. 2-adrenergic receptor for high affinity binding of salmeterol. Mol. Pharmacol. 54, 616-622 (1998).
32. Shi, L. & Javitch, J. A. The second extracellular loop of the dopamine D2 receptor lines the binding-site crevice. Proc. Natl Acad. Sci. USA 101, 440-445 (2004).
33. Klco, J. M., Wiegand, C. B., Narzinski, K. & Baranski, T. J. Essential role for the second extracellular loop in C5a receptor activation. Nature Struct. Mol. Biol. 12, 320-326 (2005).
34. Voigtlander, U. et al. Allosteric site on muscarinic acetylcholine receptors: Identification of two amino acids in the muscarinic M-2 receptor that account entirely for the M-2/M-5 subtype selectivities of some structurally diverse allosteric ligands in N-methylscopolamine-occupied receptors. Mol. Pharmacol. 64, 21-31 (2003).
35. Avlani, V. A. et al. Critical role for the second extracellular loop in the binding of both orthosteric and allosteric G protein-coupled receptor ligands. J. Biol. Chem. 282, 25677-25686 (2007).
36. 2-adrenoceptor contributes to agonist binding and receptor activation. Br. J. Pharmacol. 128, 272-274 (1999).
37. Strader, C. D. et al. Identification of 2 serine residues involved in agonist activation of the β-adrenergic-receptor. J. Biol. Chem. 264, 13572-13578 (1989).
38. 2- adrenergic receptor. J. Biol. Chem. 275, 37779-37788 (2000).
39. 2-adrenergic receptor function. Science 318, 1266-1273 (2007).
40. 2-adrenergic receptor. Proc. Natl Acad. Sci. USA 96, 12322-12327 (1999).
41. Schwartz, T. W. et al. Molecular mechanism of 7TM receptor activation - a global toggle switch model. Annu. Rev. Pharmacol. Toxicol. 46, 481-519 (2006).
42. Warne, T., Chirnside, J. & Schertler, G. F. Expression and purification of truncated, non-glycosylated turkey beta-adrenergic receptors for crystallization. Biochim. Biophys. Acta 1610, 133-140 (2003).
43. Riekel, C., Burghammer, M. & Schertler, G. Protein crystallography microdiffraction. Curr. Opin. Struct. Biol. 15, 556-562 (2005).
44. Standfuss, J. et al. Crystal structure of a thermally stable rhodopsin mutant. J. Mol. Biol. 372, 1179-1188 (2007).
45. Evans, P. Scaling and assessment of data quality. Acta Crystallogr. D 62, 72-82 (2006).
46. McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Cryst. 40, 658-674 (2007).
47. Adams, P. D. et al. PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr. D 58, 1948-1954 (2002).
48. Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron-density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
49. Kabsch, W. & Sander, G. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637 (1983).
50. 1-adrenoceptor. Mol. Pharmacol. 63, 1312-1321 (2003).
51. Donaldson, J., Brown, A. M. & Hill, S. J. Influence of rolipram on the cyclic 3′,5′-adenosine monophosphate response to histamine and adenosine in slices of guinea-pig cerebral cortex. Biochem. Pharmacol. 37, 715-723 (1988).
52. 2-adrenoceptor provide evidence for agonist-directed signaling. Mol. Pharmacol. 64, 1357-1369 (2003).