The minor binding pocket: A major player in 7TM receptor activation

Trends in Pharmacological Sciences

Volumn 31, Issue 12, 2010, Pages 567-574

  Rosenkilde, Mette M ^a   Benned Jensen, Tau ^a   Frimurer, Thomas M ^a   Schwartz, Thue W ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE A2 RECEPTOR; ANGIOTENSIN 1 RECEPTOR; BETA 2 ADRENERGIC RECEPTOR; CHEMOKINE RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; MELANOCORTIN RECEPTOR; MEMBRANE RECEPTOR; PROLINE; RETINA S ANTIGEN; SEVEN TRANSMEMBRANE RECEPTOR; UNCLASSIFIED DRUG;

ALLOSTERISM; BINDING AFFINITY; CRYSTAL STRUCTURE; HYDROGEN BOND; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; RECEPTOR BINDING; SHORT SURVEY; SIGNAL TRANSDUCTION; UPREGULATION;

ANIMALS; BINDING SITES; DRUG DELIVERY SYSTEMS; HUMANS; LIGANDS; MODELS, MOLECULAR; PROTEIN STRUCTURE, QUATERNARY; RECEPTORS, G-PROTEIN-COUPLED; SIGNAL TRANSDUCTION;

EID: 78549272001     PISSN: 01656147     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tips.2010.08.006     Document Type: Short Survey

References (61)

1. Lefkowitz R.J. Historical review: a brief history and personal retrospective of seven-transmembrane receptors. Trends Pharmacol. Sci. 2004, 25:413-422.
2. Hofmann K.P., et al. A G protein-coupled receptor at work: the rhodopsin model. Trends Biochem. Sci. 2009, 34:540-552.
3. Nygaard R., et al. Ligand binding and micro-switches in 7TM receptor structures. Trends Pharmacol. Sci. 2009, 30:249-259.
4. Palczewski K., et al. Crystal structure of rhodopsin: a G protein-coupled receptor. Science 2000, 289:739-745.
5. Li J., et al. Structure of bovine rhodopsin in a trigonal crystal form. J. Mol. Biol. 2004, 343:1409-1438.
6. Okada T., et al. The retinal conformation and its environment in rhodopsin in light of a new 2.2Å crystal structure. J. Mol. Biol. 2004, 342:571-583.
7. 2-adrenergic G protein-coupled receptor. Science 2007, 318:1258-1265.
8. 2-adrenergic receptor function. Science 2007, 318:1266-1273.
9. 2 adrenergic G-protein-coupled receptor. Nature 2007, 450:383-387.
10. Park J.H., et al. Crystal structure of the ligand-free G-protein-coupled receptor opsin. Nature 2008, 454:183-187.
11. 1-adrenergic G-protein-coupled receptor. Nature 2008, 454:486-491.
12. Altenbach C., et al. High-resolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:7439-7444.
13. Scheerer P., et al. Crystal structure of opsin in its G-protein-interacting conformation. Nature 2008, 455:497-502.
14. 2A adenosine receptor bound to an antagonist. Science 2008, 322:1211-1217.
15. Ahuja S., et al. Location of the retinal chromophore in the activated state of rhodopsin. J. Biol. Chem. 2009, 284:10190-10201.
16. Rosenbaum D.M., et al. The structure and function of G-protein-coupled receptors. Nature 2009, 459:356-363.
17. Schwartz T.W., et al. Molecular mechanism of 7TM receptor activation - a global toggle switch model. Annu. Rev. Pharmacol. Toxicol. 2006, 46:481-519.
18. Kobilka B. Agonist binding: a multistep process. Mol. Pharmacol. 2004, 65:1060-1062.
19. Huber T., Sakmar T.P. Rhodopsin's active state is frozen like a DEER in the headlights. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:7343-7344.
20. Rosenkilde M.M., Schwartz T.W. GluVII:06 - a highly conserved and selective anchor point for non-peptide ligands in chemokine receptors. Curr. Top. Med. Chem. 2006, 6:1319-1333.
21. Jensen P.C., Rosenkilde M.M. Chapter 8. Activation mechanisms of chemokine receptors. Methods Enzymol. 2009, 461:171-190.
22. Jensen P.C., et al. Molecular interaction of a potent nonpeptide agonist with the chemokine receptor CCR8. Mol. Pharmacol. 2007, 72:327-340.
23. 1 receptor. Drug Des. Discov. 1992, 9:49-67.
24. 278 in ligand binding and sodium modulation. Biochem. Pharmacol. 2000, 60:661-668.
25. 3 chemokine receptor through anchoring of a small molecule chelator ligand between TM-III, -IV, and -VI. Mol. Pharmacol. 2007, 71:930-941.
26. Tunaru S., et al. Characterization of determinants of ligand binding to the nicotinic acid receptor GPR109A (HM74A/PUMA-G). Mol. Pharmacol. 2005, 68:1271-1280.
27. Offermanns S. The nicotinic acid receptor GPR109A (HM74A or PUMA-G) as a new therapeutic target. Trends Pharmacol. Sci. 2006, 27:384-390.
28. Glusman G., et al. Sequence, structure, and evolution of a complete human olfactory receptor gene cluster. Genomics 2000, 63:227-245.
29. von Heijne G. Proline kinks in transmembrane α-helices. J. Mol. Biol. 1991, 218:499-503.
30. Elling C.E., et al. Metal ion site engineering indicates a global toggle switch model for seven-transmembrane receptor activation. J. Biol. Chem. 2006, 281:17337-17346.
31. Mirzadegan T., et al. Sequence analyses of G-protein-coupled receptors: similarities to rhodopsin. Biochemistry 2003, 42:2759-2767.
32. Devillé J., et al. An indel in transmembrane helix 2 helps to trace the molecular evolution of class A G-protein-coupled receptors. J. Mol. Evol. 2009, 68:475-489.
33. 5. A structural determinant of chemokine-induced activation. J. Biol. Chem. 2001, 276:13217-13225.
34. 1 receptor signal transduction. Regul. Pept. 2007, 140:32-36.
35. 2 induced by conformational changes in the conserved TXP motif in transmembrane helix 2. J. Biol. Chem. 2003, 278:36513-36521.
36. Benned-Jensen T., Rosenkilde M.M. Structural motifs of importance for the constitutive activity of the orphan 7TM receptor EBI2: analysis of receptor activation in the absence of an agonist. Mol. Pharmacol. 2008, 74:1008-1021.
37. Benned-Jensen T., Rosenkilde M.M. The role of transmembrane segment II in 7TM receptor activation. Curr. Mol. Pharmacol. 2009, 2:140-148.
38. Rosenkilde M.M., et al. Molecular pharmacological phenotyping of EBI2. An orphan seven-transmembrane receptor with constitutive activity. J. Biol. Chem. 2006, 281:13199-13208.
39. Ling M.K., et al. Association of feather colour with constitutively active melanocortin 1 receptors in chicken. Eur. J. Biochem. 2003, 270:1441-1449.
40. Robbins L.S., et al. Pigmentation Phenotypes of variant extension locus alleles result from point mutations that alter MSH receptor function. Cell 1993, 72:1-20.
41. Theron E., et al. The molecular basis of an avian plumage polymorphism in the wild: a melanocortin-1-receptor point mutation is perfectly associated with the melanic plumage morph of the bananaquit, Coereba flaveola. Curr. Biol. 2001, 11:550-557.
42. + channels. Nature 2008, 451:826-829.
43. Freites J.A., et al. Interface connections of a transmembrane voltage sensor. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:15059-15064.
44. Schmidt D., et al. Phospholipids and the origin of cationic gating charges in voltage sensors. Nature 2006, 444:775-779.
45. Pardo L., et al. The role of internal water molecules in the structure and function of the rhodopsin family of G protein-coupled receptors. ChemBiochem 2007, 8:19-24.
46. Kobilka B., Schertler G.F. New G-protein-coupled receptor crystal structures: insights and limitations. Trends Pharmacol. Sci. 2008, 29:79-83.
47. Nygaard R., et al. The conserved water mediated hydrogen bond network between TM-I, II, VI and VII in 7TM receptor activation. J. Biol. Chem. 2010, 285:19625-19636.
48. Patel A.B., et al. Changes in interhelical hydrogen bonding upon rhodopsin activation. J. Mol. Biol. 2005, 347:803-812.
49. Angel T.E., et al. Structural waters define a functional channel mediating activation of the GPCR, rhodopsin. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:14367-14372.
50. Okada T., et al. Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:5982-5987.
51. Miura S., Karnik S.S. Constitutive activation of angiotensin II type 1 receptor alters the orientation of transmembrane helix-2. J. Biol. Chem. 2002, 277:24299-24305.
52. Miura S., et al. TM2-TM7 interaction in coupling movement of transmembrane helices to activation of the angiotensin II type-1 receptor. J. Biol. Chem. 2003, 278:3720-3725.
53. Rosenkilde M.M., et al. Mutations along transmembrane segment II of the NK-1 receptor affect substance P competition with non-peptide antagonists but not substance P binding. J. Biol. Chem. 1994, 269:28160-28164.
54. Richman J.G., et al. Nicotinic acid receptor agonists differentially activate downstream effectors. J. Biol. Chem. 2007, 282:18028-18036.
55. Walters R.W., et al. β-Arrestin1 mediates nicotinic acid-induced flushing, but not its antilipolytic effect, in mice. J. Clin. Invest. 2009, 119:1312-1321.
56. Tunaru S., et al. PUMA-G and HM74 are receptors for nicotinic acid and mediate its anti-lipolytic effect. Nat. Med. 2003, 9:352-355.
57. Reis, R.I. and Costa-Neto, C.M. (2009) Structural aspects related to angiotensin AT1 receptor activation. In Abstracts of the 2009 Gordon Research Conference on Molecular Pharmacology: Recent Advances in Basic and Translational Research on G Protein-Coupled Receptors and Signaling.
58. Hjorth S.A., et al. Identification of peptide binding residues in the extracellular domains of the AT1 receptor. J. Biol. Chem. 1994, 269:30953-30959.
59. Baldwin J.M. The probable arrangement of the helices in G protein-coupled receptors. EMBO J. 1993, 12:1693-1703.
60. Schwartz T.W. Locating ligand-binding sites in 7TM receptors by protein engineering. Curr. Opin. Biotechnol. 1994, 5:434-444.
61. 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. Receptor Molecular Biology 1995, 366-428. Academic Press. S.C. Sealfon (Ed.).