Modes of peptide binding in G protein-coupled receptors

Neurochemical Research

Volumn 22, Issue 8, 1997, Pages 1023-1031

  Berthold, Malin ^a   Bartfai, Tamas ^a  

^a STOCKHOLM UNIVERSITY   (Sweden)

Author keywords

Agonist; Allosteric effect; Antagonist; Binding site; G protein coupled receptors; Peptide

Indexed keywords

ANGIOTENSIN 1 RECEPTOR; ANGIOTENSIN DERIVATIVE; BETA 2 ADRENERGIC RECEPTOR; GALANIN; GUANINE NUCLEOTIDE BINDING PROTEIN; MONOAMINE; NEUROKININ 1 RECEPTOR; NEUROPEPTIDE; NEUROPEPTIDE Y; NEUROTRANSMITTER; NEUROTRANSMITTER RECEPTOR; SUBSTANCE P;

ARTICLE; BINDING SITE; HORMONE RECEPTOR INTERACTION; HUMAN; NEUROTRANSMISSION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN STRUCTURE; RECEPTOR BINDING;

ANGIOTENSIN II; ANIMALS; BINDING SITES; GALANIN; GTP-BINDING PROTEINS; HUMANS; NEUROPEPTIDE Y; PROTEIN BINDING; RECEPTORS, ANGIOTENSIN; RECEPTORS, NEUROKININ-1; RECEPTORS, NEUROPEPTIDE; RECEPTORS, NEUROPEPTIDE Y; RECEPTORS, PEPTIDE; SUBSTANCE P;

EID: 0030792923     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1022483027858     Document Type: Article

References (57)

1. Schwartz, T. W., Gether, U., Schambye, H. T., and Hjorth, S. A. 1995. Molecular mechanism of action of non-peptide ligands for peptide receptors. Cur. Pharmaceut. Design. 1:325-342.
2. Monod, J., Wyman, J., and Changeux, J.-P. 1965. On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12:88-118.
3. Khorana, H. G. 1988. Bacteriorhodopsin, a membrane protein that uses light to translocate protons. J. Biol. Chem. 263:7439-7442.
4. Henderson, R., Baldwin, J. M., Ceska, T. A., Zemlin, F., Beckmann, E., and Downing, K. H. 1990. Model of the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213:899-929.
5. Unger, V. M., and Schertler, G. F. X. 1995. Low resolution structure of bovine rhodopsin determined by electron cryo-microscopy. Biophys. J. 68:1776-1786.
6. Schertler, G. F. X., Villa, C., and Henderson, R. 1993. Projection structure of rhodopsin. Nature. 362:770-772.
7. Schertler, G. F. X., and Hargrave, P. A. 1995. Projection structure of frog rhodopsin in two crystal forms. Proc. Natl. Acad. Sci. USA. 92:11578-11582.
8. Baldwin, J. M. 1993. The probable arrangements of the helices in G protein-coupled receptors. EMBO J. 12:1693-1703.
9. Strader, C. D., Fong, T. M., Tota, M., Underwood, D., and Dixon, R. A. F. 1994. Structure and function of G protein-coupled receptors. Annu. Rev. Biochem. 63:101-132.
10. Kobilka, B. K., Kobilka, T. S., Daniel, K., Regan, J. W., Caron, M. G., and Lefkowitz, R. J. 1988. Chimeric α2,β2-adrenergic receptors: Delineation of domains involved in effector coupling and ligand binding specificity. Science. 240:1310-1316.
11. Strader, C. D., Candelore, M. R., Hill, W. S., Sigal, I. S., and Dixon, R. A. F. 1989. Identification of two serine residues involved in agonist activation of the β-adrenergic receptor. J. Biol. Chem. 264:13572-13578.
12. Strader, C. D., Gaffney, T., Sugg, E. E., Rios Candelore, M., Keys, R., Patchett, A. A., and Dixon, R. A. F. 1991. Allele-specific activation of genetically engineered receptors. J. Biol. Chem. 266:5-8.
13. Schwartz, T. W. 1994. Locating ligand-binding sites in 7 TM receptors by protein engineering. Curr. Opin. Biotechn. 5:424-444.
14. Strader, C. D., Fong, T. M., Graziano, M. P., and Tota, M. R. 1995. The family of G-protein-coupled receptors. FASEB J. 9: 745-754.
15. Fong, T. M., Huang, R.-R. C., and Strader, C. D. 1992. Localization of agonist and antagonist binding domains of the human neurokinin-1 receptor. J. Biol. Chem. 267:25664-25667.
16. Yokota, Y., Akazawa, C., Ohkubo, H., and Nakanishi, S. 1992. Delineation of structural domains involved in the subtype specificity of tachykinin receptors through chimeric formation of substance P/substance K receptors. EMBO J. 11:3585-2591.
17. Gether, U., Johansen, T. E., Snider, R. M., Lowe III, J. A., Nakanishi, S., and Schwartz, T. 1993. Different binding epitopes on the NK1 receptor for substance P and a non-peptide antagonist. Nature. 362:345-348.
18. Fong, T. M., Yu, H., Huang, R.-R. C., and Strader, C. D. 1992. The extracellular domain of the neurokinin-1 receptor is required for high-affinity binding of peptides. Biochemistry. 31:11806-11811.
19. Fong, T. M., Yu, H., and Strader, C. D. 1992. Molecular basis for the species selectivity of the neurokinin-1 receptor antagonists CP-96,345 and RP67580. J. Biol. Chem. 267:25668-25671.
20. Huang, R.-R. C., Yu, H., Strader, C. D., and Fong, T. M. 1994. Interaction of substance P with the second and seventh transmembrane domains of the neurokinin-1 receptor. Biochemistry. 33: 3007-3013.
21. Li, Y.-M., Mamerakis, M., Stimson, E. R., and Maggio, J. E. 1995. Mapping peptide-binding domains of the substance P (NK-1) receptor from P388D1 cells with photolabile agonists. J. Biol. Chem. 270:1213-1220.
22. Boyd, N. D., Kage, R., Dumas, J. J., Krause, J. E., and Leeman, S. E. 1996. The peptide binding site of the substance P (NK-1) receptor localized by photoreactive analogue of substance P: pres-ence of a disulphide bond. Proc. Natl. Acad. Sci. USA. 93:433-437.
23. Girault, S., Sagan, S., Bolbach, G., LaVielle, S., and Chassaing, G. 1996. The use of photolabelled peptides to localize the substance P binding site in the human neurokinin-1 tachykinin receptor. Eur. J. Biochem. 240:215-222.
24. Fong, T. M., Cascieri, M. A., Yu, H., Bansal, A., Swain, C., and Strader, C. D. 1993. Amino-aromatic interaction between histidine 197 of the neurokinin-1 receptor and CP 96345. Nature 62:350-353.
25. Gether, U., Nilsson, L., Lowe III, J. A., and Schwartz, T. W. 1994. 2 specific residues at the top of transmembrane segment V and VI of the neurokinin-1 receptor involved in binding of the non-peptide antagonist CP 96,345. J. Biol. Chem. 269:23959-23964.
26. Joseph, M. P., Maigret, B., Bonnafous, J. C., Marie, J., and Scheraga, H. A. 1995. A computer modeling postulated mechanism for angiotensin II receptor activation. J. Protein. Chem. 14:381-398.
27. Yamano, Y., Ohyama, K., Chaki, S., Guo, D. F., and Inagami, T. 1992. Identification of amino acid residues of rat angiotensin II receptor for ligand binding by site directed mutagenesis. Biochem. Biophys. Res. Commun. 187:1426-1431.
28. Yamano, Y., Ohyama, K., Kikyo, M., Sano, T., Y., N., Inoue, Y., Nakamura, N., Morishima, I., Guo, D.-F., Hamakubo, T., and T., I. 1995. Mutagenesis and the molecular modeling of the rat angiotensin II receptor (AT1). J. Biol. Chem. 270:14024-14030.
29. Noda, K., Saad, Y., Kinoshita, A., Boyle, T. P., Graham, R. M., Husain, A., and Kamik, S. S. 1995. Tetrazole and carboxylate groups of angiotensin receptor antagonists bind to the same subsite by different mechanisms. J. Biol. Chem. 270:2284-2289.
30. Groblewski, T., Maigret, B., Nouet, S., Larguier, R., Lombard, C., Bonnafous, J. C., and Marie, J. 1995. Amino acids of the third transmembrane domain of the AT1A angiotensin II receptor are involved in the differential recognition of peptide and nonpeptide ligands. Biochem. Biophys. Res. Commun. 209:153-160.
31. Monnot, C., Bihoreau, C., Conchon, S., Curnow, K. M., Corvol, P., and Clauser, E. 1996. Polar residues in the transmembrane domains of the type 1 angiotensin II receptor are required for binding and coupling. Reconstitution of the binding site by coexpression of two deficient mutants. J. Biol. Chem. 271:1507-1513.
32. Hjorth, S. A., Schambye, H. T., Greenlee, W. J., and Schwartz, T. W. 1994. Identification of peptide binding residues in the extracellular domains of the AT1 receptor. J. Biol. Chem. 269: 30953-30959.
33. Feng, Y.-H., Noda, K., Saad, Y., Liu, X.-P., Husain, A., and S., K. S. 1995. The docking of Arg2 of angiotensin II with Asp281 of ATI receptor is essential for full agonism. J. Biol. Chem. 270: 12846-12850
34. Hunyady, L., Balla, T., and Catt, K. J. 1996. The ligand binding site of the angiotensin ATI receptor. Trends Pharmacol. Sci. 17: 135-140
35. Walker, P., Munoz, M., Martinez, R., and Peitsch, M. C. 1994. Acidic residues in extracellular loops of the human Y1 neuropeptide Y receptor are essential for ligand binding. J. Biol. Chem. 269:2863-2869
36. Blundell, T. L., Pitts, J. E., Tickle, I. J., Wood, S. P., and Wu, C.-W. 1981. X-ray analysis (1.4 Å resolution) of avian pancreatic polypeptide: Small globular protein hormone. Proc. Natl. Acad. Sci. USA. 78:4175-4179.
37. Sautel, M., Martinez, R., Munoz, M., Peitsch, M. C., Beck-Sickinger, A. G., and Walker, P. 1995. Role of a hydrophobic pocket of the human Y1 neuropeptide Y receptor in ligand binding. Mol. Cell. Endocrinol. 112:215-222
38. Sautel, M., Rudolf, K., Wittneben, H., Herzog, H., Martinez, R., Munoz, M., Eberlein, W., Engel, W., Walker, P., and Beck Sickinger, A. G. 1996. Neuropeptide Y and the nonpeptide antagonist BIBP 3226 share an overlapping binding site at the human Y1 receptor. Mol. Pharmacol. 50:285-292
39. Fisone, G., Berthold, M., Bedecs, K., Undén, A., Bartfai, T., Bertorelli, R., Consolo, S., Crawley, J., Martin, B., Nilsson, S., and Hökfelt, T. 1989. N-Terminal galanin-(1-16) fragment is an agonist at the hippocampal galanin receptor. Proc. Natl. Acad. Sci. USA. 86:9588-9591
40. Amiranoff, B., Lorinet, A. M., Yanaihara, N., and Laburthe, M. 1989. Structural requirement for galanin action in the pancreatic beta cell line Rin m 5F. Eur. J. Pharmacol. 163:205-207
41. Land, T., Langel, Ü., Löw, M., Berthold, M., Undén, A., and Bartfai, T. 1991. Linear and cyclic N-terminal galanin fragments and analogs as ligands at the hypothalamic galanin receptor. Int. J. Peptide Protein Res. 38:267-272
42. Rigler, R., Wennerberg, A., Cooke, R. M., Elofsson, A., Nilsson, L., Vogel, H., Holley, L. H., Carlquist, M., Langel, Ü., Bartfai, T., and Campbell, I. D. 1991. On the solution structure of galanin. Pages 17-25, in: Hökfelt, T., Bartfai, T., Jacobowitz, D., and Ottoson, D., (eds.), Galanin: A new multifunctional peptide in the neuro-endocrine system, McMillan Press, London.
43. Morris, M. B., Ralston, G. B., Biden, T. J., Browne, C. L., King, G. F., and Iismaa, T. P. 1995. Structural and biochemical studies of human galanin: NMR evidence for nascent helical structures in aqueous solution. Biochemistry. 34:4538-45.
44. Kask, K., Berthold, M., Kahl, U., Nordvall, G., and Bartfai, T. 1996. Delineation of the peptide binding site of the human galanin receptor. EMBO J. 15:236-244
45. Elling, C. E., Nielsen, S. M., and Schwartz, T. W. 1995. Conversion of antagonist-binding site to metal-ion site in the tachykinin NK-1 receptor. Nature. 374:74-77
46. Lee, J. A., Elliott, J. D., Sutiphong, J. A., Friesen, W. J., Ohlstein, E. H., Stadel, J. M., Gleason, J. G., and Peishoff, C. E. 1994. Tyr-129 is important to the peptide ligand affinity and selectivity of human endothelin type A receptor. Proc. Natl. Acad. Sci. USA. 91:7164-7168
47. Krystek, S. R. J., Patel, P. S., Rose, P. M., Fisher, S. M., Kienzle, B. D., Lach, D. A., Liu, E. C.-K., Lynch, J. S., Novotny, J., and Webb, M. L. 1994. Mutation of peptide binding site in transmembrane region of a G protein-coupled receptor accounts for endothelin receptor subtype selectivity. J. Biol. Chem. 269:12383-12386
48. Adachi, M., Furuichi, Y., and Miyamoto, C. 1994. Identification of a ligand-binding site of the human endothelin-A receptor and specific regions required for ligand selectivity. Eur. J. Biochem. 220:37-43.
49. Nardone, J., and Hogan, P. G. 1994. Delineation of a region in the B2 bradykinin receptor that is essential for high-affinity agonist binding. Proc. Natl. Acad. Sci. USA. 91:4417-4421
50. Novotny, E. A., Bednar, D. L., Connolly, A. A., Connor, J. R., and Stormann, T. M. 1994. Mutation of aspartate residues in the third extracellular loop of the rat B2 bradykinin receptor decreases affinity for bradykinin. Biochem. Biophys. Res. Commun. 201: 523-530.
51. Alla, S. A., Quitterer, U., Grigoriev, S., Maidhof, A., Haasemann, M., Jarnagin, K., and Müller-Esterl, W. 1996. Extracellular domains of the bradykinin B2 receptor involved in ligand binding and agonist sensing defined by anti-peptide antibodies. J. Biol. Chem. 271:1748-1755
52. Perlman, J. H., Laakkonen, L., Osman, R., and Gershengom, M. C. 1994. A model of the thyrotropin-releasing hormone (TRH) receptor binding pocket. Evidence for a second direct interaction between transmembrane helix 3 and TRH. J. Biol. Chem. 269: 23383-23386
53. Perlman, J. H., Thaw, C. N., Laakkonen, L., Bowers, C. Y., Osman, R., and Gershengom, M. C. 1994. Hydrogen bonding interaction of thyrotropin-releasing hormone (TRH) with transmembrane tyrosine 106 of the TRH receptor. J. Biol. Chem. 269:1610-1613.
54. Clackson, T., and Wells, J. A. 1995. A hot spot of binding energy in a hormone - receptor interface. Science. 267:383-386
55. Beinborn, M., Lee, Y.-M., McBride, E. W., Quinn, S. M., and Kopin, A. S. 1993. A single amino acid of the cholecystokinin-B/gastrin receptor determines specificity for non-peptide antagonists. Nature. 362:348-350
56. Fathi, Z., Benya, R. V., Shapira, H., Jensen, R. T., and J.F., B. 1993. The fifth transmembrane segment of the neuromedin B receptor is critical for high affinity neuromedin B binding. J. Biol. Chem. 268:14622-14626
57. Cascieri, M. A., Fong, T. M., and Strader, C. A. 1995. Molecular characterization of a common binding site for small molecules within the transmembrane domain of G-protein coupled receptors. J. Pharmacol. Toxicol. Methods. 33:179-185