A database of mutants and effects of site-directed mutagenesis experiments on G protein-coupled receptors

Proteins: Structure, Function and Genetics

Volumn 26, Issue 1, 1996, Pages 81-94

  Kristiansen, Kurt ^a   Dahl, Svein G ^a   Edvardsen, Øyvind ^a  

^a UNIVERSITY OF TROMSØ   (Norway)

Author keywords

database; G protein coupled receptors; information storage and retrieval; Internet; ligand receptor interactions; sequence alignment; signal transduction; Site directed mutagenesis; software; World Wide Web

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; MUTANT PROTEIN;

ARTICLE; COMPUTER NETWORK; DATA BASE; INFORMATION RETRIEVAL; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN ANALYSIS; RECEPTOR BINDING; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; COMPUTER COMMUNICATION NETWORKS; COMPUTERS; GTP-BINDING PROTEINS; INFORMATION SYSTEMS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; RECEPTORS, CELL SURFACE; SEQUENCE ALIGNMENT;

EID: 0029845242     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199609)26:1<81::AID-PROT8>3.0.CO;2-J     Document Type: Article

References (55)

1. 2 receptor. Proc. Natl. Acad. Sci. U.S.A. 88:8111-8115, 1991.
2. 1a receptor and ligands. Protein Eng. 6:691-700, 1993.
3. Dahl, S.G., Edvardsen, Ø. Molecular modeling of dopamine receptors. In: "Dopamine Receptors and Transporters. Pharmacology, Structure and Function." Niznik, H.B. (ed.). New York: Marcel Decker, 1994:265-281.
4. Rands, E., Candelore, M.R., Cheung, A.H., Hill, W.S., Strader, C.D., Dixon, R.A.F. Mutational analysis of β-adrenergic receptor glycosylation. J. Biol. Chem. 265:10759-10764, 1990.
5. 2-adrenergic receptor delays onset of agonist-promoted desensitization. Nature 333:370-373, 1988.
6. 2-adrenergic receptor. Phosphorylation of the receptor and regulation of its mRNA level. J. Biol. Chem. 264:16786-16792, 1989.
7. Lameh, J., Philip, M., Sharma, Y.K., Moro, O., Ramachandran, J., Sadée, W. Hm1 muscarinic cholinergic receptor internalization requires a domain in the third cytoplasmic loop. J. Biol. Chem. 267:13406-13412, 1992.
8. 2-adrenergic receptor in agonist-induced down-regulation of the receptor. Proc. Natl. Acad. Sci. U.S.A. 87:5089-5093, 1990.
9. 2-adrenergic receptor. J. Biol. Chem. 264:7564-7569, 1989.
10. Dixon, R.A.F., Sigal, I.S., Candelore, M.R., Register, R.B., Scattergood, W., Rands, E., Strader, C.D. Structural features required for ligand binding to the β-adrenergic receptor. EMBO J. 6:3269-3275, 1987.
11. Franke, R.R., Sakmar, T.P., Oprian, D.D., Khorana, H.G. A single amino acid substitution in rhodopsin (lysine 248→leucine) prevents activation of transducin. J. Biol. Chem. 263:2119-2122, 1988.
12. Min, K.C., Zvyaga, T.A., Cypess, A.M., Sakmar, T.P. Characterization of mutant rhodopsins responsible for autosomal dominant retinitis pigmentosa. J. Biol. Chem. 268: 9400-9404, 1993.
13. 2-adrenergic receptor within the fourth transmembrane domain alters ligand binding and functional properties of the receptor. J. Biol. Chem. 268:23116-23121, 1993.
14. Vu, T.-K.H., Hung, D.T., Wheaton, V.I., Coughlin, S.R. Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation. Cell 64:1057-1068, 1991.
15. Robinson, P.R., Cohen, G.B., Zhukovsky, E.A., Oprian, D.D. Constitutive active mutants of rhodopsin. Neuron 9:719-725, 1992
16. Strader, C.D., Sigal, I.S., Register, R.B., Candelore, M.R., Rands, E., Dixon, R.A.F. Identification of residues required for ligand binding to the β-adrenergic receptor. Proc. Natl. Acad. Sci. U.S.A. 84:4384-4388, 1987.
17. Dixon, R.A.F., Sigal, I.S., Strader, C.D. Structure-function analysis of the β-adrenergic receptor. Cold Spring Harbor Symp Quant Biol 53:487-497, 1988.
18. 2 adrenergic receptor increases its affinity for a family of β receptor antagonists. J. Biol. Chem. 266: 15488-15492, 1991.
19. Chan, T., Lee, M., Sakmar, T.P. Introduction of hydroxyl-bearing amino acids causes bathochromic spectral shifts in rhodopsin. J. Biol. Chem. 267:9478-9480, 1992.
20. 2 receptor from a human to a rat pharmacology. FEBS Lett. 307:324-328, 1992.
21. Guiramand, J., Montmayeur, J.-P., Ceraline, J., Bhatia, M., Borrelli, E. Alternative splicing of the dopamine D2 receptor directs specificity of coupling to G-proteins. J. Biol. Chem. 270:7354-7358, 1995.
22. Bhogal, N., Donnelly, D., Findlay, J.B.C. The ligand binding site of the neurokinin 2 receptor: Site-directed mutagenesis and identification of neurokinin A binding residues in the human neurokinin 2 receptor. J. Biol. Chem. 269:27269-27274, 1994.
23. Lee, J.A., Elliott, J.D., Sutiphong, J.A., Friesen, W.J., Ohlstein, E.H., Stadel, J.M., Gleason, J.G., Peishoff, C.E. Tyr-129 is important to the peptide ligand affinity and selectivity of human endothelin type A receptor. Proc. Natl. Acad. Sci. U.S.A. 91:7164-7168, 1994.
24. Krystek Jr., S.R., Patel, P.S., Rose, P.M., Fisher, S.M., Kienzle, B.K., Lach, D.A., Liu, E.C.-K., Lynch, J.S., Novotny, J., Webb, M.L. 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, 1994.
25. Zhou, W., Flanagan, C., Ballesteros, J.A., Konvicka, K., Davidson, J.S., Weinstein, H., Millar, R.P., Sealfon, S.C. A reciprocal mutation supports helix 2 and helix 7 proximity in the gonadotropin-releasing hormone receptor. Mol. Pharmacol. 45:165-170, 1994.
26. 1A angiotensin II receptor is essential for its coupling to phospholipase C. J. Biol. Chem. 269:20815-20818, 1994.
27. Donnelly, D., Findlay, J.B.C., Blundell, T.L. The evolution and structure of aminergic G protein-coupled receptors. Recept. Channels 2:61-78, 1994.
28. Perlman, J.H., Laakkonen, L., Osman, R., Gershengorn, M.C. 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, 1994.
29. 2A receptors: Ergolines require an aromatic residue at position 340 for high affinity binding. Mol. Pharmacol. 47:450-457, 1995.
30. Strader, C.D., Fong, T.M., Tota, M.R., Underwood, D., Dixon, R.A.F. Structure and function of G protein-coupled receptors. Annu. Rev. Biochem. 63:101-132, 1994.
31. Savarese, T.M., Fraser, C.M. In vitro mutagenesis and the search for structure-function relationships among G protein-coupled receptors. Biochem. J. 283:1-19, 1992.
32. Baldwin, J.M. Structure and function of receptors coupled to G proteins. Curr. Opin. Cell. Biol. 6:180-190, 1994.
33. Gudermann, T., Nürnberg, B., Schultz, G. Receptors and G proteins as primary components of transmembrane signal transduction. Part 1. G-protein-coupled receptors: Structure and function. Clin. Invest. 73:51-63, 1995.
34. Offermanns, S., Schultz, G. Complex information processing by the transmembrane signaling system involving G proteins. Naunyn Schmiedebergs Arch. Pharmacol. 350: 329-338, 1994.
35. 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. Methods Neurosci. 25:366-428, 1994.
36. Kolakowski, L.F. Jr. GCRDb: A G protein-coupled receptor database. Recept. Channels 2:1-7, 1994.
37. Baldwin, J.M. The probable arrangement of the helices in G protein-coupled receptors. EMBO J. 12:1693-1703, 1993.
38. Oliveira, L., Paiva, A.C.M., Vriend, G. A common motif in G-protein-coupled seven transmembrane helix receptors. J. Comput. Aided Mol. Design 7:649-658, 1993.
39. Attwood, T.K., Findlay, J.B.C. Fingerprinting G-protein-coupled receptors. Protein Eng. 7:195-203, 1994.
40. Raymond, J.R. Hereditary and acquired defects in signaling through the hormone-receptor-G protein complex. [Editorial]. Am. J. Physiol. 266:F163-F174, 1994.
41. Aho, A.V., Kernighan, B.W., Weinberger, P. "The AWK Programming Language." Reading, MA: Addison Wesley, 1988.
42. Berners-Lee, T.J., Cailliau, R., Groff, J.-F., Pollermann, B. In: "Electronic Networking: Research, Applications and Policy." Vol. 2. Westport, CT: Meckler Publishing, 1992: 52-58.
43. Boutell, T. Available by anonymous ftp from rtfm.mit.edu [18.181.0.24] in /pub/usenet/news.answers/www/faq or by WWW on http:/www.boutell.com/faq/. World Wide Web Frequently Asked Questions 1995.
44. December, J., Randall, N. "The World Wide Web Unleashed." Indianapolis: Sams Publishing, 1994.
45. Bairoch, A., Boeckmann, B. The SWISS-PROT protein sequence data bank. Nucleic Acids Res. 19:2247-2249, 1991.
46. Program Manual for the Wisconsin Package, Version 8, September 1994, Genetics Computer Group, 575 Science Drive, Madison, Wisconsin, USA 53711, 1994.
47. Fasman, K.H., Cuticchia, A.J., Kingsbury, D.T. The GDB human genome data base anno 1994. Nucleic Acids Res. 22:3462-3469, 1994.
48. Appel, R.D., Bairoch, A., Hochstrasser, D.F. A new generation of information retrieval tools for biologists: the example of the ExPASy WWW server. Trends Biochem. Sci. 19:258-260, 1994.
49. Pearson, P., Francomano, C., Foster, P., Bocchini, C., Li, P., McKusick, V., Hopkins, J. The status of online mendelian inheritance in man (OMIM) medio 1994. Nucleic Acids Res. 22:3470-3473, 1994.
50. Probst, W.C., Snyder, L.A., Schuster, D.I., Brosius, J., Sealfon, S.C. Sequence alignment of the G-protein coupled receptor superfamily. DNA Cell Biol. 11:1-20, 1992.
51. Zuurmond, H. The files mutants.list and mutanta.lit are available by anonymous ftp from swift.EMBL-Heidelberg.DE in tm7/help. TM7 Database, 1994.
52. 194. Biochem. Biophys. Res. Commun. 203:1096-1101, 1994.
53. Laakkonen, L.J., Guarnieri, F., Perlman, J.H., Gershengorn, M.C., Osman, R. Model of the complex of thyrotropin releasing hormone with its receptor. [Abstract]. Biophys. J. 68:A446, 1995.
54. Schertler, G.F.X., Villa, C., Henderson, R. Projection structure of rhodopsin. Nature 362:770-772, 1993.
55. Unger, V.M., Schertler, G.F.X. Low resolution structure of bovine rhodopsin determined by electron cryo-microscopy. Biophys. J. 68:1776-1786, 1995.