The structural basis for agonist and partial agonist action on a β1-adrenergic receptor

Nature

Volumn 469, Issue 7329, 2011, Pages 241-245

  Warne, Tony ^a   Moukhametzianov, Rouslan ^a   Baker, Jillian G ^b   Nehmé, Rony ^a   Edwards, Patricia C ^a   Leslie, Andrew G W ^a   Schertler, Gebhard F X ^a,c   Tate, Christopher G ^a  

^a MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

^b UNIVERSITY OF NOTTINGHAM   (United Kingdom)

^c PAUL SCHERRER INSTITUTE   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

BETA 1 ADRENERGIC RECEPTOR; BETA 1 ADRENERGIC RECEPTOR STIMULATING AGENT; CARMOTEROL; DOBUTAMINE; G PROTEIN COUPLED RECEPTOR; ISOPRENALINE; SALBUTAMOL;

ASTHMA; CARDIOVASCULAR DISEASE; CELL ORGANELLE; CRYSTAL STRUCTURE; DISEASE TREATMENT; HORMONE; HYDROGEN; HYPERTENSION; INHIBITION; LIGAND; MEMBRANE; POULTRY; PROTEIN;

ARTICLE; COMPLEX FORMATION; CRYSTAL STRUCTURE; HYDROGEN BOND; LIGAND BINDING; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; RECEPTOR BINDING; STRUCTURE ANALYSIS; TURKEY (BIRD); X RAY DIFFRACTION;

ADRENERGIC BETA-1 RECEPTOR AGONISTS; ADRENERGIC BETA-1 RECEPTOR ANTAGONISTS; ALBUTEROL; AMPHETAMINES; ANIMALS; BINDING SITES; CATECHOLAMINES; CRYSTALLOGRAPHY, X-RAY; DOBUTAMINE; DRUG DESIGN; DRUG PARTIAL AGONISM; HYDROGEN BONDING; HYDROXYQUINOLINES; ISOPROTERENOL; LIGANDS; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN STABILITY; RECEPTORS, ADRENERGIC, BETA-1; SERINE; STRUCTURE-ACTIVITY RELATIONSHIP; TURKEYS;

MELEAGRIS GALLOPAVO;

EID: 78651405537     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature09746     Document Type: Article

References (42)

1. Evans, B. A. et al. Ligand-directed signallingat β-adrenoceptors. Br. J. Pharmacol. 159, 1022-1038(2010).
2. Rosenbaum, D. M., Rasmussen, S. G. & Kobilka, B. K. Thestructureandfunctionof G-protein-coupled receptors. Nature 459, 356-363 (2009).
3. Ballesteros, J. A. & Weinstein, H. Integrated methodsfortheconstruction ofthree dimensional modelsandcomputational probingof structurefunction relations in G protein-coupled receptors. Methods Neurosci. 25, 366-428 (1995).
4. Strader, C. D. et al. Conserved asparticacid residues 79and 113 of the β-adrenergic receptor have different roles in receptor function. J. Biol. Chem. 263, 10267-10271 (1988).
5. 2-adrenoceptor contributes to agonist binding and receptor activation. Br. J. Pharmacol. 128, 272-274 (1999).
6. 2-adrenergic receptor. J. Biol. Chem. 275, 37779-37788 (2000).
7. Strader, C. D. et al. Identification oftwoserine residues involved in agonist activation of the beta-adrenergic receptor. J. Biol. Chem. 264, 13572-13578 (1989).
8. Wieland, K. et al. InvolvementofAsn-293 instereospecificagonistrecognitionand in activation of the beta 2-adrenergic receptor. Proc. Natl Acad. Sci. USA 93, 9276-9281 (1996).
9. Suryanarayana, S. & Kobilka, B. K. Aminoacidsubstitutionsatposition 312 in the seventh hydrophobic segment of the beta 2-adrenergic receptor modifyligand-bindingspecificity. Mol. Pharmacol. 44, 111-114 (1993).
10. 2- selectiveagonist TA-2005. Mol. Pharmacol. 53, 128-134 (1998).
11. Isogaya, M. et al. Identification of a keyaminoacid of theβ2-adrenergicreceptor for high affinity bindingof salmeterol. Mol. Pharmacol. 54, 616-622 (1998).
12. 2-adrenergic G protein-coupled receptor. Science 318, 1258-1265 (2007).
13. 1-adrenergicG-protein- coupled receptor. Nature 454, 486-491 (2008).
14. 2-adrenergic receptor. Structure 16, 897-905 (2008).
15. Wacker, D. et al. Conservedbindingmodeof human β 2adrenergicreceptorinverse agonistsandantagonistrevealed byX-raycrystallography. J. Am. Chem. Soc. 132, 11443-11445 (2010).
16. Tate, C. G. & Schertler, G. F. Engineering G protein-coupled receptors to facilitate their structure determination. Curr. Opin. Struct Biol. 19, 386-395 (2009).
17. Kobilka, B. K. & Deupi, X. Conformational complexity of G-protein-coupled receptors. Trends Pharmacol. Sci. 28, 397-406 (2007).
18. Park, J. H. Crystal structure of the ligand-free G-protein-coupled receptor opsin. Nature 454, 183-187 (2008).
19. Scheerer, P. et al. Crystal structure of opsin in its G-protein-interacting conformation. Nature 455, 497-502 (2008).
20. 1-receptortransgenicmice. Mol. Pharmacol. 60, 712-717 (2001).
21. s. Eur. J. Pharmacol. 411, 141-147 (2001).
22. 2- adrenergic receptor gene on coronary artery disease. J. Am. Coll. Cardiol. 52, 1381-1388 (2008).
23. Serrano-Vega, M. J. & Tate, C. G. Transferability of thermostabilizing mutations between β-adrenergic receptors. Mol. Membr. Biol. 26, 385-396 (2009).
24. Serrano-Vega, M. J., Magnani, F., Shibata, Y. & Tate, C. G. Conformationa thermostabilization of the β1-adrenergic receptor in a detergent-resistantform. Proc. Natl Acad. Sci. USA 105, 877-882 (2008).
25. 1-adrenergic receptor. Biophys. J. 99, 568-577 (2010).
26. 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).
27. 2 adrenergic G-protein-coupled receptor. Nature 450, 383-387 (2007).
28. Williams, R. S. & Bishop, T. Selectivityofdobutamineforadrenergic receptor subtypes: in vitro analysis by radioligand binding. J. Clin. Invest 67, 1703-1711 (1981).
29. 2-adrenergic receptorsuggestsa Role oftransmembrane helixV in agonist-specific conformational changes. J. Mol. Recognit 22, 307-318 (2009).
30. Warne, T., Serrano-Vega, M. J., Tate, C. G. & Schertler, G. F. Development and crystallization of a minimal thermostabilised G protein-coupled receptor Protein Expr. Purif. 65, 204-213 (2009).
31. Leslie, A. G. W. The integration of macromoleculardiffraction data. Acta Crystallogr. D 62, 48-57 (2006).
32. Evans, P. Scaling and assessment of data quality. Acta Crystallogr. D 62, 72-82 (2006).
33. McCoy, A. J. et al. Phasercrystal lographics of tware. J. Appl. Cryst 40, 658-674 (2007).
34. Murshudov, G. N., Vagin, A. A. & Dodson, E. J. Refinementof macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53, 240-255 (1997).
35. Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D 66, 486-501 (2010).
36. Schüttelkopf, A. W. & van Aalten, D. M. PRODRG: a tool for high-throughput crystallographyof protein-ligand complexes. Acta Crystallogr. D60, 1355-1363 (2004).
37. McDonald, I. K. & Thornton, J. M. Satisfyinghydrogen bondingpotentialin proteins. J. Mol. Biol. 238, 777-793 (1994).
38. Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methodsforbuilding protein models in electron-density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
39. Davis, I. W. et al. Mol Probity: all-atomcontact sandstruct urevalidation for proteins and nucleic acids. Nucleic Acids Res. 35, W375-W383 (2007).
40. 1-adrenoceptor. Mol. Pharmacol. 63, 1312-1321 (2003).
41. Warne, T., Chirnside, J. & Schertler, G. F. Expression and purification oftruncated, non-glycosylated turkey beta-adrenergic receptors forcrystallization. Biochim. Biophys. Acta 1610, 133-140 (2003).
42. 50) of an enzymatic reaction. Biochem. Pharmacol. 22, 3099-3108 (1973).