Identification of the amino acid subsets accounting for the ligand binding specificity of a glutamate receptor

Neuron

Volumn 17, Issue 5, 1996, Pages 979-990

  Paas, Yoav ^a   Eisenstein, Miriam ^a   Medevielle, François ^b   Teichberg, Vivian I ^a   Devillers Thiéry, Anne ^b  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

^b CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

6 CYANO 7 NITRO 2,3 QUINOXALINEDIONE; AMINO ACID; BINDING PROTEIN; GLUTAMATE RECEPTOR; GLUTAMIC ACID; KAINIC ACID; LIGAND; NEUROTRANSMITTER RECEPTOR;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; HUMAN; HUMAN CELL; LIGAND BINDING; MUTANT; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS;

EID: 17144450204     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0896-6273(00)80228-7     Document Type: Article

References (52)

1. Altschul, S.F., Gish, W., Miller, W., Myers, E.W., and Lipman, D.J. (1990). Basic local alignment search tool. J. Mol. Biol. 215, 403-410.
2. Ames, G.F.-L. (1986). Bacterial periplasmic transport system: structure, mechanism and evolution. Annu. Rev. Biochem. 55, 397-425.
3. Beall, J.A., and Mitchell, G.F. (1986). Identification of a particular antigen from a parasite cDNA library using antibodies affinity purified from selected proteins of Western blots. J. Immunol. Meth. 86, 217-223.
4. Bennett, J.A., and Dingledine, R. (1995). Topology profile for a glutamate receptor: three transmembrane domains and a channel-lining reentrant membrane loop. Neuron 14, 373-384.
5. Berland, C.R., Sigurskjold, B.W., Stoffer, B., Frandsen, T.P., and Svensson, B. (1995). Thermodynamics of inhibitor binding to mutant forms of glucoamylasefrom Aspergillus niger determined by isothermal titration calorimetry. Biochemistry 34, 10153-10161.
6. Bourne, H.R., Sanders, D.A., and McCormick, F. (1991). The GTPase superfamily: conserved structure and molecular mechanism. Nature 349, 117-127.
7. Bowie, J.U., Luthy, R., and Eisenberg, D. (1991 ). A method to identify protein sequences that fold into a known three-dimensional structure. Science 253, 164-170.
8. Branden, C., and Tooze, J. (1991). Introduction to Protein Structure (London: Garland Publishing, Incorporated).
9. Cockcroft, V.B., Orteils, M.O., Thomas, P., and Lunt, G.G. (1993). Homologies and disparities of glutamate receptors: a critical analysis. Neurochem. Int. 23, 583-594.
10. Gasic, G.P., and Hollmann M. (1992). Molecular neurobiology of glutamate receptors. Annu. Rev. Physiol. 54, 507-536.
11. Gorodinsky, A., Paas, Y., and Teichberg, V.I. (1993). A ligand binding study of the interactions of guanine nucleotides with non-NMDA receptors. Neurochem. Int. 23, 285-291.
12. Gregor, P., Eshhar, N., Ortega, A., and Teichberg, V.I. (1988). Isolation, immunochemical characterization and localization of the kainate sub-class of glutamate receptor from chick cerebellum. EMBO J. 7, 2673-2679.
13. Gregor, P., Mano, I., Maoz, I., McKeown, M., and Teichberg, V.I. (1989). Molecular structure of the chick cerebellar kainate binding subunit of a putative glutamate receptor. Nature 342, 689-692.
14. Hanks, S.K., Quinn, A.-M., and Hunter, T. (1988). The protein kinase family: conserved features and deduced phylogeny of catalytic domains. Science 247, 42-52.
15. Hirai, H., Kirsch, J., Laube, B., Setz, H., and Kuhse, J. (1996). The glycine binding site of the N-methyl-D-aspartate receptor subunit NR1: identification of novel determinants of co-agonist potentiation in the extracellular M3-M4 loop region. Proc. Natl. Acad. Sci. USA 93, 6031-6036.
16. Hollmann, M., and Heinemann, S. (1994). Cloned glutamate receptors. Annu. Rev. Neurosci. 17, 31-108.
17. Hollmann, M., Maron, C., and Heinemann, S. (1994). N-glycosylation site tagging suggests a three transmembrane domain topology for the glutamate receptor GluR1. Neuron 13, 1331-1343.
18. Kang, C.-H., Shin, W.-C., Yamagata, Y., Gokcen, S., Ames, G.F.-L., and Kim, S.-H. (1991). Crystal structure of the lysine-, arginine-, ornithine-binding protein (LAO) from Salmonella typhimurium at 2.7-Å resolution. J. Biol. Chem. 266, 23893-23899.
19. Kuryatov, A., Laube, B., Setz, H., and Kuhse, J. (1994). Mutational analysis of the glycine-binding site of the NMDA receptor: structure similarity with bacterial amino acid-binding proteins. Neuron 12, 1291-1300.
20. Kuusinen, A., Arvola, M., and Keinänen, K. (1995). Molecular dissection of the agonist binding site of an AMPA receptor. EMBO J. 14, 6327-6332.
21. Levitzki, A. (1978). Quantitative Aspects of Allosteric Mechanism (Berlin: Springer-Verlag).
22. Li, F., Owens, N., and Verdoorn, T.A. (1995). Functional effects of mutations in the putative agonist binding region of recombinant α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors. Mol. Pharmacol. 47, 148-154.
23. Luecke, H., and Quiocho, F. (1990). High specificity of a phosphate transport protein determined by hydrogen bonds. Nature 347, 402-406.
24. Mano, I., Lamed, Y., and Teichberg, V.I. (1996). A venus flytrap mechanism for activation and desensitization of α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors. J. Biol. Chem. 271, 15299-15302.
25. Nakanishi, N., Shneider, N.A., and Axel, R. (1990). A family of glutamate receptor genes: evidence for the formation of heteromultimeric receptors with distinct channel properties. Neuron 5, 569-581.
26. Oh, B.-H., Pandit, J., Kang, C.-H., Nikaido, K., Gokcen, S., Ames, G.F.-L., and Kim, S.-H. (1993). Three-dimensional structure of the periplasmic lysine/arginine/ornithine-binding protein with and without a ligand. J. Biol. Chem. 268, 11348-11355.
27. Oh, B.-H., Kang, C.-H., De Bondt, H., Kim, S.-H., Nikaido, K., Joshi, A.K.S., and Ames, G.F.-L. (1994). The bacterial periplasmic histidine-binding protein: structure/function analysis of the ligand-binding site and comparison with related proteins. J. Biol. Chem. 269, 4135-4143.
28. O'Hara, P.J., Sheppard, P.O., Thogersen, H., Venezia, D., Haldeman, B.A., McGrane, V., Houamed, K.M., Thomsen, C., Gilbert, T.L., and Mulvihill, E.R. (1993). The ligand-binding domain in metabotropic glutamate receptors is related to bacterial periplasmic binding proteins. Neuron 11, 41-52.
29. Paas, Y., and Teichberg, V.I. (1992). The ligand binding site of the chick cerebellar glial kainate receptor. Int. J. Dev. Neurosci. 10 (Suppl. 1), 47.
30. Paas, Y., Devillers-Thiéry, A., Changeux, J.-P., Maoz, I., and Teichberg, V.I. (1994). The guanine nucleotide binding site of the chick cerebellar kainate binding protein and its relevance to the ligand binding site of glutamate receptors. J. Neurochem. 63 (Suppl. 1), S1D.
31. Paas, Y., Devillers-Thiéry, A., Changeux, J.-P., Medevielle, F., and Teichberg, V.I. (1996). Identification of an extracellular motif involved in the binding of guanine nucleotides by a glutamate receptor. EMBO J. 15, 1548-1556.
32. Pai, E.F., Kabsch, W., Krengel, U., Holmes, K.C., John, J., and Wittinghofer, A. (1989). Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation. Nature 341, 209-214.
33. Pai, E.F., Krengel, U., Petsko, G.A., Goody, R.S., Kabsch, W., and Wittinghofer, A. (1990). Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 Å resolution: implications for the mechanism of GTP hydrolysis. EMBO J. 9, 2351-2359.
34. Partin, K.M., Bowie, D., and Mayer, M.L. (1995). Structural determinants of allosteric regulation in alternatively spliced AMPA receptors. Neuron 14, 833-843.
35. Pearson, W.R., and Lipman, D.J. (1988). Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA 85, 2444-2448.
36. Pin, J.P., and Duvoisin, R. (1995). The metabotropic glutamate receptors: structure and functions. Neuropharmacology 34, 1-26.
37. Quiocho, F.A. (1990). Atomic structures of periplasmic binding proteins and the high-affinity active transport system in bacteria. Phil. Trans. Roy. Soc. (Lond.) B 326, 341-351.
38. Rost, B., and Sander, C. (1994). Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19, 55-72.
39. Schreiber, G., and Fersht, A.R. (1995). Energetics of protein-protein interactions: analysis of the Barnase-Barstar interface by single mutations and double mutant cycles. J. Mol. Biol. 248, 478-486.
40. Smith, T.F., and Waterman, M.S. (1981). Identification of common molecular subsequences. J. Mol. Biol. 147, 195-197.
41. Sommer, B., Keinänen, K., Verdoorn, T.A., Wisden, W., Burnashev, N., Herb, A., Köhler, M., Takagi, T., Sakmann, B., and Seeburg, P.H. (1990). Flip and flop: a cell-specific functional switch in glutamate-operated channels of the CNS. Science 249, 1580-1585.
42. Stern-Bach, Y., Bettler, B., Hartley, M., Sheppard, P.O., O'Hara, P.J., and Heinemann, S.F. (1994). Agonist selectivity of glutamate receptors is specified by two domains structurally related to bacterial amino acid-binding proteins. Neuron 13, 1345-1357.
43. Sutcliffe, M.J., Wo, Z.G., and Oswald, R.E. (1996). Three-dimensional models of non-NMDA glutamate receptors. Biophys. J. 70, 1575-1589.
44. Swick, A.G., Janicot, T., Cheneval-Kastelic, T., McLenithan, J.C., and Lane, M.D. (1992). Promoter-cDNA-directed heterologous protein expression in Xenopus laevis oocytes. Proc. Natl. Acad. Sci. USA 89, 1812-1816.
45. Towbin, H., Staehelin, T., and Gordon, J. (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354.
46. Uchino, S., Sakimura, K., Nagahari, K., and Mishina, M. (1992). Mutations in a putative agonist binding region of the AMPA-selective glutamate receptor channel. FEBS Lett. 308, 253-257.
47. Wada, K., Dechesne, C.J., Shimasaki, S., King, R.G., Kusano, K., Buonanno, A., Hampson, D.R., Banner, C., Wenthold, R.J., and Nakatani, Y. (1989). Sequence and expression of a frog brain complementary DNA encoding a kainate-binding protein. Nature 342, 684-688.
48. Wafford, K.A., Kathoria, M., Bain, C.J., Marshall, B., Le Bourdelles, B., Kemp, J.A., and Whiting, P.J. (1995). Identification of amino acids in the N-methyl-D-aspartate receptor NR1 subunit that contribute to the glycine binding site. Mol. Pharmacol. 47, 374-380.
49. Wang, Z., Choudhary, A., Ledvina, P.S., and Quiocho, F.A. (1994). Fine tuning the specificity of the periplasmic phosphate transport receptor. J. Biol. Chem. 269, 25091-25094.
50. Wo, Z.G., and Oswald, R.E. (1994). Transmembrane topology of two kainate receptor subunits revealed by N-glycosylation. Proc. Natl. Acad. Sci. USA 91, 7154-7158.
51. Wo, Z.G., and Oswald, R.E. (1995). A topological analysis of goldfish kainate receptors predicts three transmembrane segments. J. Biol. Chem. 270, 2000-2009.
52. Wyman, J., Jr. (1964). Linked functions and reciprocal effects in hemoglobin: a second look. Adv. Prot. Chem. 19, 223-286.