GPCR engineering yields high-resolution structural insights into β2-adrenergic receptor function

Science

Volumn 318, Issue 5854, 2007, Pages 1266-1273

  Rosenbaum, Daniel M ^a   Cherezov, Vadim ^b   Hanson, Michael A ^b   Rasmussen, Søren G F ^a   Foon, Sun Thian ^a   Kobilka, Tong Sun ^a   Choi, Hee Jung ^a   Yao, Xiao Jie ^a   Weis, William I ^a   Stevens, Raymond C ^b   Kobilka, Brian K ^a  

^a STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

3 ISOPROPYLAMINO 1 (7 METHYL 4 INDANYLOXY) 2 BUTANOL; ADRENALIN; AMINO ACID DERIVATIVE; BETA 2 ADRENERGIC RECEPTOR; CARAZOLOL; CATECHOLAMINE; FORMOTEROL; G PROTEIN COUPLED RECEPTOR; ISOPRENALINE; LYSOZYME; RHODOPSIN; SALBUTAMOL;

ENERGETICS; HORMONE; HYDROGEN; PROTEIN;

ARTICLE; BINDING AFFINITY; CELL SURFACE; CRYSTALLIZATION; DRUG BINDING; HUMAN; HYDROGEN BOND; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN ENGINEERING; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STRUCTURE; WILD TYPE;

ADRENERGIC BETA-AGONISTS; ADRENERGIC BETA-ANTAGONISTS; AMINO ACID SEQUENCE; BACTERIOPHAGE T4; BINDING SITES; CELL LINE; CELL MEMBRANE; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DRUG INVERSE AGONISM; HUMANS; IMMUNOGLOBULIN FAB FRAGMENTS; LIGANDS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MURAMIDASE; PROPANOLAMINES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, ADRENERGIC, BETA-2; RECOMBINANT FUSION PROTEINS;

EID: 36448978229     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1150609     Document Type: Article

References (50)

1. H. G. Khorana, J. Biol. Chem. 267, 1 (1992).
2. B. K. Kobilka, X. Deupi, Trends Pharmacol. Sci. 28, 397 (2007).
3. V. Cherezov et al., Science 318, 1258 (2007); published online 25 October 2007 (10.1126/science.1150577).
4. 2AR.
5. S. Granier et al., J. Biol. Chem. 282, 13895 (2007).
6. B. K. Kobilka et al., Science 240, 1310 (1988).
7. X. J. Zhang, J. A. Wozniak, B. W. Matthews, J. Mol. Biol. 250, 527 (1995).
8. L. H.Weaver, B. W. Matthews, J. Mol. Biol. 193, 189 (1987).
9. Ballesteros-Weinstein numbering is used throughout the text as superscripts to the protein numbering. Within each helix is a single, most conserved residue among the class A GPCRs. This residue is designated x.50, where x is the number of the transmembrane helix. All other residues on that helix are numbered relative to this conserved position.
10. T. Okada et al., J. Mol. Biol. 342, 571 (2004).
11. M. Matsumura, W. J. Becktel, M. Levitt, B. W. Matthews, Proc. Natl. Acad. Sci. U.S.A. 86, 6562 (1989).
12. F. Horn et al., Nucleic Acids Res. 31, 294 (2003).
13. Materials and methods and supplementary figures are available as supporting material on Science Online.
14. D. R. Smyth, M. K. Mrozkiewicz, W. J. McGrath, P. Listwan, B. Kobe, Protein Sci. 12, 1313 (2003).
15. U. Gether et al., J. Biol. Chem. 272, 2587 (1997).
16. S. G. Rasmussen et al., Mol. Pharmacol. 56, 175 (1999).
17. P. Ghanouni et al., J. Biol. Chem. 276, 24433 (2001).
18. P. Ghanouni, J. J. Steenhuis, D. L. Farrens, B. K. Kobilka, Proc. Natl. Acad. Sci. U.S.A. 98, 5997 (2001).
19. G. Swaminath et al., J. Biol. Chem. 279, 686 (2004).
20. G. Swaminath et al., J. Biol. Chem. 280, 22165 (2005).
21. X. Yao et al., Nat. Chem. Biol. 2, 417 (2006).
22. P. Samama, S. Cotecchia, T. Costa, R. J. Lefkowitz, J. Biol. Chem. 268, 4625 (1993).
23. S. G. F. Rasmussen et al., Nature, published online 21 October 2007; 10.1038/nature06325.
24. Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
25. J. A. Ballesteros et al., J. Biol. Chem. 276, 29171 (2001).
26. C. D. Strader et al., Proc. Natl. Acad. Sci. U.S.A. 84, 4384 (1987).
27. C. D. Strader et al., J. Biol. Chem. 263, 10267 (1988).
28. S. Suryanarayana, B. K. Kobilka, Mol. Pharmacol. 44, 111 (1993).
29. G. Liapakis et al., J. Biol. Chem. 275, 37779 (2000).
30. P. Chelikani et al., Proc. Natl. Acad. Sci. U.S.A. 104, 7027 (2007).
31. Y. Sugimoto et al., J. Pharmacol. Exp. Ther. 301, 51 (2002).
32. T. Frielle, K. W. Daniel, M. G. Caron, R. J. Lefkowitz, Proc. Natl. Acad. Sci. U.S.A. 85, 9494 (1988).
33. C. D. Strader, M. R. Candelore, W. S. Hill, I. S. Sigal, R. A. Dixon, J. Biol. Chem. 264, 13572 (1989).
34. K. Wieland, H. M. Zuurmond, C. Krasel, A. P. Ijzerman, M. J. Lohse, Proc. Natl. Acad. Sci. U.S.A. 93, 9276 (1996).
35. H. Kikkawa, M. Isogaya, T. Nagao, H. Kurose, Mol. Pharmacol. 53, 128 (1998).
36. U. Gether et al., EMBO J. 16, 6737 (1997).
37. Y. X. Tao, A. N. Abell, X. Liu, K. Nakamura, D. L. Segaloff, Mol. Endocrinol. 14, 1272 (2000).
38. A. D. Jensen et al., J. Biol. Chem. 276, 9279 (2001).
39. L. Shi et al., J. Biol. Chem. 277, 40989 (2002).
40. L. Pardo, X. Deupi, N. Dolker, M. L. Lopez-Rodriguez, M. Campillo, ChemBioChem 8, 19 (2007).
41. L. S. Barak, L. Menard, S. S. Ferguson, A. M. Colapietro, M. G. Caron, Biochemistry 34, 15407 (1995).
42. M. J. Lohse, C. Hoffmann, V. O. Nikolaev, J. P. Vilardaga, M. Bunemann, Adv. Protein Chem. 74, 167 (2007).
43. W. L. DeLano, The PyMOL Molecular Graphics System (DeLano Scientific, Palo Alto, CA, 2002), www.pymol.org.
44. A. W. Schüttelkopf, D. M. F. van Aalten, Acta Crystallogr. D Biol. Crystallogr. D60, 1355 (2004).
45. M. J. Zuscik, J. E. Porter, R. Gaivin, D. M. Perez, J. Biol. Chem. 273, 3401 (1998).
46. F. Z. Chung, C. D. Wang, P. C. Potter, J. C. Venter, C. M. Fraser, J. Biol. Chem. 263, 4052 (1988).
47. O. Moro, M. S. Shockley, J. Lameh, W. Sadee, J. Biol. Chem. 269, 6651 (1994).
48. S. A. Green, G. Cole, M. Jacinto, M. Innis, S. B. Liggett, J. Biol. Chem. 268, 23116 (1993).
49. A. M. Gabilondo et al., Proc. Natl. Acad. Sci. U.S.A. 94, 12285 (1997).
50. 2AR- T4L have been deposited in the Protein Data Bank with identification code 2RH1.