Crystallizing thinking about the β2-adrenergic receptor

Molecular Pharmacology

Volumn 73, Issue 5, 2008, Pages 1333-1338

  Shukla, Arun K ^a   Sun, Jin Peng ^a   Lefkowitz, Robert J ^a  

^a DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BETA 2 ADRENERGIC RECEPTOR; CARAZOLOL; CARVEDILOL; G PROTEIN COUPLED RECEPTOR; RHODOPSIN; CARBAZOLE DERIVATIVE; PROPANOLAMINE DERIVATIVE;

CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; DRUG MECHANISM; DRUG STRUCTURE; NONHUMAN; NOTE; PRIORITY JOURNAL; PROTEIN EXPRESSION; ARTICLE; CHEMISTRY; HUMAN; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; STRUCTURAL HOMOLOGY; X RAY CRYSTALLOGRAPHY;

CARBAZOLES; CRYSTALLOGRAPHY, X-RAY; HUMANS; PROPANOLAMINES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECEPTORS, ADRENERGIC, BETA-2; RHODOPSIN; STRUCTURAL HOMOLOGY, PROTEIN;

EID: 42449139192     PISSN: 0026895X     EISSN: 15210111     Source Type: Journal    
DOI: 10.1124/mol.108.045849     Document Type: Note

References (28)

1. Ballesteros JA, Jensen AD, Liapakis G, Rasmussen SG, Shi L, Gether U, and Javitch JA (2001) 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.
2. Caron MG, Srinivasan Y, Pitha J, Kociolek K, and Lefkowitz RJ (1979) Affinity chromatography of the β-adrenergic receptor. J Biol Chem 254:2923-2927.
3. Cherezov V, Rosenbaum DM, Hanson MA, Rasmussen SG, Thian FS, Kobilka TS, Choi HJ, Kuhn P, Weis WI, Kobilka BK, et al. (2007) High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor. Science 318:1258-1265.
4. Cotecchia S, Exum S, Caron MG, and Lefkowitz RJ (1990) Regions of the alpha 1-adrenergic receptor involved in coupling to phosphatidylinositol hydrolysis and enhanced sensitivity of biological function. Proc Natl Acad Sci U S A 87:2896-2900.
5. Day PW, Rasmussen SG, Parnot C, Fung JJ, Masood A, Kobilka TS, Yao XJ, Choi HJ, Weis WI, Rohrer DK, et al. (2007) A monoclonal antibody for G protein-coupled receptor crystallography. Nat Methods 4:927-929.
6. DeWire SM, Ahn S, Lefkowitz RJ, and Shenoy SK (2007) Beta-arrestins and cell signaling. Annu Rev Physiol 69:483-510.
7. Dixon RA, Kobilka BK, Strader DJ, Benovic JL, Dohlman HG, Frielle T, Bolanowski MA, Bennett CD, Rands E, Diehl RE, et al. (1986) Cloning of the gene and cDNA for mammalian beta-adrenergic receptor and homology with rhodopsin. Nature 321:75-79.
8. Dohlman HG, Thorner J, Caron MG, and Lefkowitz RJ (1991) Model systems for the study of seven-transmembrane-segment receptors. Annu Rev Biochem 60:653-688.
9. Faham S and Bowie JU (2002) Bicelle crystallization: a new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure. J Mol Biol 316:1-6.
10. 2-adrenoceptor: insights from fluorescence resonance energy transfer studies. J Biol Chem 282:13895-13905.
11. Hargrave PA, McDowell JH, Curtis DR, Wang JK, Juszczak E, Fong SL, Rao JK, and Argos P (1983) The structure of bovine rhodopsin. Biophys Struct Mech 9:235-244.
12. Hebert TE, Moffett S, Morello JP, Loisel TP, Bichet DG, Barret C, and Bouvier M (1996) A peptide derived from a β2-adrenergic receptor transmembrane domain inhibits both receptor dimerization and activation. J Biol Chem 271:16384-16392.
13. Hunte C and Michel H (2002) Crystallisation of membrane proteins mediated by antibody fragments. Curr Opin Struct Biol 12:503-508.
14. Lefkowitz RJ (2007) Seven transmembrane receptors: something old, something new. Acta Physiol (Oxf) 190:9-19.
15. Milligan G (2004) G protein-coupled receptor dimerization: function and ligand pharmacology. Mol Pharmacol 66:1-7.
16. Ovchinnikov YuA (1982) Rhodopsin and bacteriorhodopsin: structure-function relationships. FEBS Lett 148:179-191.
17. Palczewski K, Kumasaka T, Hori T, Behnke CA, Motoshima H, Fox BA, Le Trong I, Teller DC, Okada T, Stenkamp RE, et al. (2000) Crystal structure of rhodopsin: a G protein-coupled receptor. Science 289:739-745.
18. Rasmussen SG, Choi HJ, Rosenbaum DM, Kobilka TS, Thian FS, Edwards PC, Burghammer M, Ratnala VR, Sanishvili R, Fischetti RF, et al. (2007) Crystal structure of the human beta2 adrenergic G-protein-coupled receptor. Nature 450:383-387.
19. Rosenbaum DM, Cherezov V, Hanson MA, Rasmussen SG, Thian FS, Kobilka TS, Choi HJ, Yao XJ, Weis WI, Stevens RC, et al. (2007) GPCR engineering yields high-resolution structural insights into beta2-adrenergic receptor function. Science 318:1266-1272.
20. Salahpour A, Angers S, Mercier JF, Lagacé M, Marullo S, and Bouvier M (2004) Homodimerization of the β2-adrenergic receptor as a prerequisite for cell surface targeting. J Biol Chem 279:33390- 33397.
21. Salom D, Lodowski DT, Stenkamp RE, Le Trong I, Golczak M, Jastrzebska B, Harris T, Ballesteros JA, and Palczewski K (2006) Crystal structure of a photoactivated deprotonated intermediate of rhodopsin. Proc Natl Acad Sci U S A 103:16123-16128.
22. Samama P, Cotecchia S, Costa T, and Lefkowitz RJ (1993) A mutation-induced activated state of the β2-adrenergic receptor. Extending the ternary complex model. J Biol Chem 268:4625-4636.
23. Shi L, Liapakis G, Xu R, Guarnieri F, Ballesteros JA, and Javitch JA 92002)Beta2 adrenergic receptor activation. Modulation of the proline kink in transmembrane 6 by a rotamer toggle switch. J Biol Chem 277:40989-40996.
24. Spiegel AM (1998) Introduction to G-protein-coupled signal transduction and human disease, in G Proteins, Receptors, and Diseases (Spiegel AM ed) pp 1-22, Humana Press, Totowa, NJ.
25. Strader CD, Candelore MR, Hill WS, Dixon RA, and Sigal IS (1988) A single amino acid substitution in the β-adrenergic receptor promotes partial agonist activity from antagonists. J Biol Chem 264:16470-16477.
26. Suryanarayana S and Kobilka BK (1993) Amino acid substitutions at position 312 in the seventh hydrophobic segment of the beta 2-adrenergic receptor modify ligand-binding specificity. Mol Pharmacol 44:111-114.
27. Whorton MR, Bokoch MP, Rasmussen SG, Huang B, Zare RN, Kobilka B, and Sunahara RK (2007) A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein. Proc Natl Acad Sci U S A 104:7682-7687.
28. Wisler JW, DeWire SM, Whalen EJ, Violin JD, Drake MT, Ahn S, Shenoy SK, and Lefkowitz RJ (2007) A unique mechanism of β-blocker action: carvedilol stimulates β-arrestin signaling. Proc Natl Acad Sci U S A 104:16657-16662.