메뉴 건너뛰기




Volumn 18, Issue 3, 2004, Pages 428-438

Emerging structural explanations of ionotropic glutamate receptor function

Author keywords

Channel gating; Crystal structure; Molecular dynamics; NMR dynamics; Receptor desensitization

Indexed keywords

IONOTROPIC RECEPTOR; POTASSIUM CHANNEL;

EID: 1542373622     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.03-0873rev     Document Type: Review
Times cited : (46)

References (100)
  • 1
    • 0032578635 scopus 로고    scopus 로고
    • Structure of a glutamate-receptor ligand-binding core in complex with kainate
    • Armstrong, N., Sun, Y., Chen, G. Q., and Gouaux, E. (1998) Structure of a glutamate-receptor ligand-binding core in complex with kainate. Nature (London) 395, 913-917
    • (1998) Nature (London) , vol.395 , pp. 913-917
    • Armstrong, N.1    Sun, Y.2    Chen, G.Q.3    Gouaux, E.4
  • 2
    • 0033636314 scopus 로고    scopus 로고
    • Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: Crystal structures of the GluR2 ligand binding core
    • Armstrong, N., and Gouaux, E. (2000) Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core. Neuron 28, 165-181
    • (2000) Neuron , vol.28 , pp. 165-181
    • Armstrong, N.1    Gouaux, E.2
  • 3
    • 0036968894 scopus 로고    scopus 로고
    • Structural basis for AMPA receptor activation and ligand selectivity: Crystal structures of five agonist complexes with the GluR2 ligand-binding core
    • Hogner, A., Kastrup, J., Jin, R., Liljefors, T., Mayer, M., Egebjerg, J., Larsen, I., and Gouaux, E. (2002) Structural basis for AMPA receptor activation and ligand selectivity: crystal structures of five agonist complexes with the GluR2 ligand-binding core. J. Mol. Biol. 322, 93-109
    • (2002) J. Mol. Biol. , vol.322 , pp. 93-109
    • Hogner, A.1    Kastrup, J.2    Jin, R.3    Liljefors, T.4    Mayer, M.5    Egebjerg, J.6    Larsen, I.7    Gouaux, E.8
  • 4
    • 0035943408 scopus 로고    scopus 로고
    • Mechanisms for ligand binding to GluR0 ion channels: Crystal structures of the glutamate and serine complexes and a closed apo state
    • Mayer, M. L., Olson, R., and Gouaux, E. (2001) Mechanisms for ligand binding to GluR0 ion channels: crystal structures of the glutamate and serine complexes and a closed apo state. J. Mol. Biol. 311, 815-836
    • (2001) J. Mol. Biol. , vol.311 , pp. 815-836
    • Mayer, M.L.1    Olson, R.2    Gouaux, E.3
  • 5
    • 0037468424 scopus 로고    scopus 로고
    • Three-dimensional structure of the ligand-binding core of GluR2 in complex with the agonist (S)-ATPA: Implications for receptor subunit selectivity
    • Lunn, M. L., Hogner, A., Stensbol, T. B., Gouaux, E., Egebjerg, J., and Kastrup, J. S. (2003) Three-dimensional structure of the ligand-binding core of GluR2 in complex with the agonist (S)-ATPA: implications for receptor subunit selectivity. J. Med. Chem. 46, 872-875
    • (2003) J. Med. Chem. , vol.46 , pp. 872-875
    • Lunn, M.L.1    Hogner, A.2    Stensbol, T.B.3    Gouaux, E.4    Egebjerg, J.5    Kastrup, J.S.6
  • 6
    • 0037448433 scopus 로고    scopus 로고
    • Competitive antagonism of AMPA receptors by ligands of different classes: Crystal structure of ATPO bound to the GluR2 ligand-binding core, in comparison with DNQX
    • Hogner, A., Greenwood, J. R., Liljefors, T., Lunn, M. L., Egebjerg, J., Larsen, I. K., Gouaux, E., and Kastrup, J. S. (2003) Competitive antagonism of AMPA receptors by ligands of different classes: crystal structure of ATPO bound to the GluR2 ligand-binding core, in comparison with DNQX. J. Med. Chem. 46, 214-221
    • (2003) J. Med. Chem. , vol.46 , pp. 214-221
    • Hogner, A.1    Greenwood, J.R.2    Liljefors, T.3    Lunn, M.L.4    Egebjerg, J.5    Larsen, I.K.6    Gouaux, E.7    Kastrup, J.S.8
  • 7
    • 0037207136 scopus 로고    scopus 로고
    • Mechanism of activation and selectivity in a ligand-gated ion channel: Structural and functional studies of GluR2 and quisqualate
    • Jin, R., Horning, M., Mayer, M. L., and Gouaux, E. (2002) Mechanism of activation and selectivity in a ligand-gated ion channel: structural and functional studies of GluR2 and quisqualate. Biochemistry 41, 15635-15643
    • (2002) Biochemistry , vol.41 , pp. 15635-15643
    • Jin, R.1    Horning, M.2    Mayer, M.L.3    Gouaux, E.4
  • 8
    • 0037032411 scopus 로고    scopus 로고
    • GluR2 ligand-binding core complexes: Importance of the isoxazolol moiety and 5-substituent for the binding mode of AMPA-type agonists
    • Kasper, C., Lunn, M. L., Liljefors, T., Gouaux, E., Egebjerg, J., and Kastrup, J. S. (2002) GluR2 ligand-binding core complexes: importance of the isoxazolol moiety and 5-substituent for the binding mode of AMPA-type agonists. FEBS Lett. 531, 173-178
    • (2002) FEBS Lett. , vol.531 , pp. 173-178
    • Kasper, C.1    Lunn, M.L.2    Liljefors, T.3    Gouaux, E.4    Egebjerg, J.5    Kastrup, J.S.6
  • 9
    • 0038037859 scopus 로고    scopus 로고
    • Mechanisms of activation, inhibition and specificity: Crystal structures of the NMDA receptor NR1 ligand-binding core
    • Furukawa, H., and Gouaux, E. (2003) Mechanisms of activation, inhibition and specificity: crystal structures of the NMDA receptor NR1 ligand-binding core. EMBO J. 22, 2873-2885
    • (2003) EMBO J. , vol.22 , pp. 2873-2885
    • Furukawa, H.1    Gouaux, E.2
  • 11
    • 0029966280 scopus 로고    scopus 로고
    • Three-dimensional models of non-NMDA glutamate receptors
    • Sutcliffe, M. J., Wo, Z. G., and Oswald, R. E. (1996) Three-dimensional models of non-NMDA glutamate receptors. Biophys. J. 70, 1575-1589
    • (1996) Biophys. J. , vol.70 , pp. 1575-1589
    • Sutcliffe, M.J.1    Wo, Z.G.2    Oswald, R.E.3
  • 12
    • 0028559605 scopus 로고
    • Agonist selectivity of glutamate receptors is specified by two domains structurally related to bacterial amino acid-binding proteins
    • 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
    • (1994) Neuron , vol.13 , pp. 1345-1357
    • Stern-Bach, Y.1    Bettler, B.2    Hartley, M.3    Sheppard, P.O.4    O'Hara, P.J.5    Heinemann, S.F.6
  • 13
    • 0032541434 scopus 로고    scopus 로고
    • AMPA receptors and bacterial periplasmic amino acid-binding proteins share the ionic mechanism of ligand recognition
    • Lampinen, M., Pentikainen, O., Johnson, M. S., and Keinanen, K. (1998) AMPA receptors and bacterial periplasmic amino acid-binding proteins share the ionic mechanism of ligand recognition. EMBO J. 17, 4704-4711
    • (1998) EMBO J. , vol.17 , pp. 4704-4711
    • Lampinen, M.1    Pentikainen, O.2    Johnson, M.S.3    Keinanen, K.4
  • 14
    • 0035451726 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the conformational changes of the glutamate receptor ligand-binding core in the presence of glutamate and kainate
    • Mendieta, J., Ramirez, G., and Gago, F. (2001) Molecular dynamics simulations of the conformational changes of the glutamate receptor ligand-binding core in the presence of glutamate and kainate. Proteins 44, 460-469
    • (2001) Proteins , vol.44 , pp. 460-469
    • Mendieta, J.1    Ramirez, G.2    Gago, F.3
  • 15
    • 0037143575 scopus 로고    scopus 로고
    • Structural mobility of the extracellular ligand-binding core of an ionotropic glutamate receptor. Analysis of NMR relaxation dynamics
    • McFeeters, R. L., and Oswald, R. E. (2002) Structural mobility of the extracellular ligand-binding core of an ionotropic glutamate receptor. Analysis of NMR relaxation dynamics. Biochemistry 41, 10472-10481
    • (2002) Biochemistry , vol.41 , pp. 10472-10481
    • McFeeters, R.L.1    Oswald, R.E.2
  • 16
    • 0036154304 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the ligand-binding domain of the ionotropic glutamate receptor GluR2
    • Arinaminpathy, Y., Sansom, M. S., and Biggin, P. C. (2002) Molecular dynamics simulations of the ligand-binding domain of the ionotropic glutamate receptor GluR2. Biophys. J. 82, 676-683
    • (2002) Biophys. J. , vol.82 , pp. 676-683
    • Arinaminpathy, Y.1    Sansom, M.S.2    Biggin, P.C.3
  • 18
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang, Y., Lee, A., Chen, J., Cadene, M., Chait, B. T., and MacKinnon, R. (2002) Crystal structure and mechanism of a calcium-gated potassium channel. Nature (London) 417, 515-522
    • (2002) Nature (London) , vol.417 , pp. 515-522
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 20
    • 0038752614 scopus 로고    scopus 로고
    • The principle of gating charge movement in a voltage-dependent K(+) channel
    • Jiang, Y., Ruta, V., Chen, J., Lee, A., and MacKinnon, R. (2003) The principle of gating charge movement in a voltage-dependent K(+) channel. Nature (London) 423, 42-48
    • (2003) Nature (London) , vol.423 , pp. 42-48
    • Jiang, Y.1    Ruta, V.2    Chen, J.3    Lee, A.4    MacKinnon, R.5
  • 23
    • 0038625032 scopus 로고    scopus 로고
    • Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic adjustment of agonist-induced conformational changes
    • Armstrong, N., Mayer, M., and Gouaux, E. (2003) Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic adjustment of agonist-induced conformational changes. Proc. Natl. Acad. Sci. USA 100, 5736-5741
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5736-5741
    • Armstrong, N.1    Mayer, M.2    Gouaux, E.3
  • 24
    • 0031677656 scopus 로고    scopus 로고
    • Probing the ligand binding domain of the GluR2 receptor by proteolysis and deletion mutagenesis defines domain boundaries and yields a crystallizable construct
    • Chen, G. Q., Sun, Y., Jin, R., and Gouaux, E. (1998) Probing the ligand binding domain of the GluR2 receptor by proteolysis and deletion mutagenesis defines domain boundaries and yields a crystallizable construct. Protein Sci. 7, 2623-2630
    • (1998) Protein Sci. , vol.7 , pp. 2623-2630
    • Chen, G.Q.1    Sun, Y.2    Jin, R.3    Gouaux, E.4
  • 25
    • 0038219813 scopus 로고    scopus 로고
    • Probing the function, conformational plasticity, and dimer-dimer contacts of the GluR2 ligand-binding core: Studies of 5-substituted willardines and GluR2 S1S2 in the crystal
    • Jin, R., and Gouaux, E. (2003) Probing the function, conformational plasticity, and dimer-dimer contacts of the GluR2 ligand-binding core: studies of 5-substituted willardines and GluR2 S1S2 in the crystal. Biochemistry 42, 5201-5213
    • (2003) Biochemistry , vol.42 , pp. 5201-5213
    • Jin, R.1    Gouaux, E.2
  • 28
    • 0032101276 scopus 로고    scopus 로고
    • Expression of an N-methyl-D-aspartate-type receptor by human and rat osteoblasts and osteoclasts suggests a novel glutamate signaling pathway in bone
    • Patton, A. J., Genever, P. G., Birch, M. A., Suva, L. J., and Skerry, T. M. (1998) Expression of an N-methyl-D-aspartate-type receptor by human and rat osteoblasts and osteoclasts suggests a novel glutamate signaling pathway in bone. Bone 22, 645-649
    • (1998) Bone , vol.22 , pp. 645-649
    • Patton, A.J.1    Genever, P.G.2    Birch, M.A.3    Suva, L.J.4    Skerry, T.M.5
  • 29
    • 15844394296 scopus 로고    scopus 로고
    • Differential expression of glutamate receptor subtypes in rat pancreatic islets
    • Weaver, C. D., Yao, T. L., Powers, A. C., and Verdoorn, T. A. (1996) Differential expression of glutamate receptor subtypes in rat pancreatic islets. J. Biol. Chem. 271, 12977-12984
    • (1996) J. Biol. Chem. , vol.271 , pp. 12977-12984
    • Weaver, C.D.1    Yao, T.L.2    Powers, A.C.3    Verdoorn, T.A.4
  • 31
    • 0032055026 scopus 로고    scopus 로고
    • Glutamate receptors are expressed by bone cells and are involved in bone resorption
    • Chenu, C., Serre, C. M., Raynal, C., Burt-Pichat, B., and Delmas, P. D. (1998) Glutamate receptors are expressed by bone cells and are involved in bone resorption. Bone 22, 295-299
    • (1998) Bone , vol.22 , pp. 295-299
    • Chenu, C.1    Serre, C.M.2    Raynal, C.3    Burt-Pichat, B.4    Delmas, P.D.5
  • 32
    • 0027504390 scopus 로고
    • Activation of nociceptive reflexes by peripheral kainate receptors
    • Ault, B., and Hildebrand, L. M. (1993) Activation of nociceptive reflexes by peripheral kainate receptors. J. Pharmacol. Exp. Ther. 265, 927-932
    • (1993) J. Pharmacol. Exp. Ther. , vol.265 , pp. 927-932
    • Ault, B.1    Hildebrand, L.M.2
  • 33
    • 0029052635 scopus 로고
    • Localization and activation of glutamate receptors in unmyelinated axons of rat glabrous skin
    • Carlton, S. M., Hargett, G. L., and Coggeshall, R. E. (1995) Localization and activation of glutamate receptors in unmyelinated axons of rat glabrous skin. Neurosci. Lett. 197, 25-28
    • (1995) Neurosci. Lett. , vol.197 , pp. 25-28
    • Carlton, S.M.1    Hargett, G.L.2    Coggeshall, R.E.3
  • 34
    • 0032527491 scopus 로고    scopus 로고
    • Molecular and immunochemical characterization of the ionotropic glutamate receptors in the rat heart
    • Gill, S. S., Pulido, O. M., Mueller, R. W., and McGuire, P. F. (1998) Molecular and immunochemical characterization of the ionotropic glutamate receptors in the rat heart. Brain Res. Bull. 46, 429-434
    • (1998) Brain Res. Bull. , vol.46 , pp. 429-434
    • Gill, S.S.1    Pulido, O.M.2    Mueller, R.W.3    McGuire, P.F.4
  • 35
    • 0028935057 scopus 로고
    • Ionotropic glutamate receptors-focus on non-NMDA receptors
    • Jorgensen, M., Tygesen, C. K., and Andersen, P. H. (1995) Ionotropic glutamate receptors-focus on non-NMDA receptors. Pharmacol. Toxicol. 76, 312-319
    • (1995) Pharmacol. Toxicol. , vol.76 , pp. 312-319
    • Jorgensen, M.1    Tygesen, C.K.2    Andersen, P.H.3
  • 36
    • 0025221685 scopus 로고
    • A family of glutamate receptor genes: Evidence for the formation of heteromultimeric receptors with distinct channel properties
    • Nakanishi, N., Schneider, 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
    • (1990) Neuron , vol.5 , pp. 569-581
    • Nakanishi, N.1    Schneider, N.A.2    Axel, R.3
  • 39
    • 0033576612 scopus 로고    scopus 로고
    • Functional characterization of a potassium-selective prokaryotic glutamate receptor
    • Chen, G. Q., Cui, C., Mayer, M. L., and Gouaux, E. (1999) Functional characterization of a potassium-selective prokaryotic glutamate receptor. Nature (London) 402, 817-821
    • (1999) Nature (London) , vol.402 , pp. 817-821
    • Chen, G.Q.1    Cui, C.2    Mayer, M.L.3    Gouaux, E.4
  • 41
    • 0034884750 scopus 로고    scopus 로고
    • Functional assembly of AMPA and kainate receptors is mediated by several discrete protein-protein interactions
    • Ayalon, G., and Stern-Bach, Y. (2001) Functional assembly of AMPA and kainate receptors is mediated by several discrete protein-protein interactions. Neuron 31, 103-113
    • (2001) Neuron , vol.31 , pp. 103-113
    • Ayalon, G.1    Stern-Bach, Y.2
  • 42
    • 0032523002 scopus 로고    scopus 로고
    • Evidence for a tetrameric structure of recombinant NMDA receptors
    • Laube, B., Kuhse, J., and Betz, H. (1998) Evidence for a tetrameric structure of recombinant NMDA receptors. J. Neurosci. 18, 2954-2961
    • (1998) J. Neurosci. , vol.18 , pp. 2954-2961
    • Laube, B.1    Kuhse, J.2    Betz, H.3
  • 43
    • 0032567729 scopus 로고    scopus 로고
    • A tetrameric subunit stoichiometry for glutamate receptor-channel complex
    • Mano, I., and Teichberg, V. I. (1998) A tetrameric subunit stoichiometry for glutamate receptor-channel complex. NeuroReport 9, 327-331
    • (1998) NeuroReport , vol.9 , pp. 327-331
    • Mano, I.1    Teichberg, V.I.2
  • 44
    • 0032486422 scopus 로고    scopus 로고
    • The tetrameric structure of a glutamate receptor channel
    • Rosenmund, C., Stern-Bach, Y., and Stevens, C. F. (1998) The tetrameric structure of a glutamate receptor channel. Science 280, 1596-1599
    • (1998) Science , vol.280 , pp. 1596-1599
    • Rosenmund, C.1    Stern-Bach, Y.2    Stevens, C.F.3
  • 45
    • 0035923431 scopus 로고    scopus 로고
    • First images of a glutamate receptor ion channel: Oligomeric state and molecular dimensions of GluRB homomers
    • Safferling, M., Tichelaar, W., Kummerle, G., Jouppila, A., Kuusinen, A., Keinanen, K., and Madden, D. R. (2001) First images of a glutamate receptor ion channel: oligomeric state and molecular dimensions of GluRB homomers. Biochemistry 40, 13948-13953
    • (2001) Biochemistry , vol.40 , pp. 13948-13953
    • Safferling, M.1    Tichelaar, W.2    Kummerle, G.3    Jouppila, A.4    Kuusinen, A.5    Keinanen, K.6    Madden, D.R.7
  • 46
    • 0026766877 scopus 로고
    • Structures and properties of seven isoforms of the NMDA receptor generated by alternative splicing
    • Sugihara, H., Moriyoshi, K., Ishii, T., Masu, M., and Nakanishi, S. (1992) Structures and properties of seven isoforms of the NMDA receptor generated by alternative splicing. Biochem. Biophys. Res. Commun. 185, 826-832
    • (1992) Biochem. Biophys. Res. Commun. , vol.185 , pp. 826-832
    • Sugihara, H.1    Moriyoshi, K.2    Ishii, T.3    Masu, M.4    Nakanishi, S.5
  • 47
    • 0025995296 scopus 로고
    • RNA editing in brain controls a determinant of ion flow in glutamate-gated channels
    • Sommer, B., Köhler, M., Sprengel, R., and Seeburg, P. H. (1991) RNA editing in brain controls a determinant of ion flow in glutamate-gated channels. Cell 67, 11-19
    • (1991) Cell , vol.67 , pp. 11-19
    • Sommer, B.1    Köhler, M.2    Sprengel, R.3    Seeburg, P.H.4
  • 49
    • 0032967642 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptor at 4.6 A resolution: Transverse tunnels in the channel wall
    • Miyazawa, A., Fujiyoshi, Y., Stowell, M., and Unwin, N. (1999) Nicotinic acetylcholine receptor at 4.6 A resolution: transverse tunnels in the channel wall. J. Mol. Biol. 288, 765-786
    • (1999) J. Mol. Biol. , vol.288 , pp. 765-786
    • Miyazawa, A.1    Fujiyoshi, Y.2    Stowell, M.3    Unwin, N.4
  • 50
    • 0028819612 scopus 로고
    • Topology profile for a glutamate receptor: Three transmembrane domains and a channel-lining re-entrant membrane loop
    • Bennett, J. A., and Dingledine, R. (1995) Topology profile for a glutamate receptor: Three transmembrane domains and a channel-lining re-entrant membrane loop. Neuron 14, 373-384
    • (1995) Neuron , vol.14 , pp. 373-384
    • Bennett, J.A.1    Dingledine, R.2
  • 51
    • 0028596211 scopus 로고
    • N-Glycosylation site tagging suggests a three transmembrane domain topology for the glutamate receptor GluR1
    • 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
    • (1994) Neuron , vol.13 , pp. 1331-1343
    • Hollmann, M.1    Maron, C.2    Heinemann, S.3
  • 52
    • 0028364252 scopus 로고
    • Transmembrane topology of two kainate receptor subunits revealed by N-glycosylation
    • 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
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7154-7158
    • Wo, Z.G.1    Oswald, R.E.2
  • 53
    • 0028965140 scopus 로고
    • Unraveling the modular design of glutamate-gated ion channels
    • Wo, Z. G., and Oswald, R. E. (1995) Unraveling the modular design of glutamate-gated ion channels. Trends Neurosci. 18, 161-168
    • (1995) Trends Neurosci. , vol.18 , pp. 161-168
    • Wo, Z.G.1    Oswald, R.E.2
  • 54
    • 0032006313 scopus 로고    scopus 로고
    • N-terminal domains in the NR2 subunit control desensitization of NMDA receptors
    • Krupp, J. J., Vissel, B., Heinemann, S. F., and Westbrook, G. L. (1998) N-terminal domains in the NR2 subunit control desensitization of NMDA receptors. Neuron 20, 317-327
    • (1998) Neuron , vol.20 , pp. 317-327
    • Krupp, J.J.1    Vissel, B.2    Heinemann, S.F.3    Westbrook, G.L.4
  • 55
    • 0032006303 scopus 로고    scopus 로고
    • Glycine-independent NMDA receptor desensitization: Localization of structural determinants
    • Villarroel, A., Regalado, M. P., and Lerm, J. (1998) Glycine-independent NMDA receptor desensitization: localization of structural determinants. Neuron 20, 329-339
    • (1998) Neuron , vol.20 , pp. 329-339
    • Villarroel, A.1    Regalado, M.P.2    Lerm, J.3
  • 56
    • 0346668335 scopus 로고    scopus 로고
    • A novel anterograde trafficking signal present in the N-terminal extracellular domain of ionotropic glutamate receptors
    • Xia, H., von Zastrow, M., and Malenka, R. C. (2002) A novel anterograde trafficking signal present in the N-terminal extracellular domain of ionotropic glutamate receptors. J. Biol. Chem. 277, 47765-47769
    • (2002) J. Biol. Chem. , vol.277 , pp. 47765-47769
    • Xia, H.1    Von Zastrow, M.2    Malenka, R.C.3
  • 57
    • 0035793597 scopus 로고    scopus 로고
    • Assembly and ligand binding properties of the water-soluble extracellular domains of the glutamate receptor I subunit
    • Wells, G. B., Lin, L., Jeanclos, E. M., and Anand, R. (2001) Assembly and ligand binding properties of the water-soluble extracellular domains of the glutamate receptor I subunit. J. Biol. Chem. 276, 3031-3036
    • (2001) J. Biol. Chem. , vol.276 , pp. 3031-3036
    • Wells, G.B.1    Lin, L.2    Jeanclos, E.M.3    Anand, R.4
  • 58
    • 0033546277 scopus 로고    scopus 로고
    • Subtype-specific assembly of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor subunits is mediated by their n-terminal domains
    • Leuschner, W. D., and Hoch, W. (1999) Subtype-specific assembly of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor subunits is mediated by their n-terminal domains. J. Biol. Chem. 274, 16907-16916
    • (1999) J. Biol. Chem. , vol.274 , pp. 16907-16916
    • Leuschner, W.D.1    Hoch, W.2
  • 59
    • 0032878510 scopus 로고    scopus 로고
    • Oligomerization and ligand-binding properties of the ectodomain of the alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor subunit GluRD
    • Kuusinen, A., Abele, R., Madden, D. R., and Keinanen, K. (1999) Oligomerization and ligand-binding properties of the ectodomain of the alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor subunit GluRD. J. Biol. Chem. 274, 28937-28943
    • (1999) J. Biol. Chem. , vol.274 , pp. 28937-28943
    • Kuusinen, A.1    Abele, R.2    Madden, D.R.3    Keinanen, K.4
  • 60
    • 0032584656 scopus 로고    scopus 로고
    • SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR1 subunit
    • Leonard, A. S., Davare, M. A., Horne, M. C., Garner, C. C., and Hell, J. W. (1998) SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR1 subunit. J. Biol. Chem. 273, 19518-19524
    • (1998) J. Biol. Chem. , vol.273 , pp. 19518-19524
    • Leonard, A.S.1    Davare, M.A.2    Horne, M.C.3    Garner, C.C.4    Hell, J.W.5
  • 61
    • 0033860051 scopus 로고    scopus 로고
    • Ligand-gated ion channel interactions with cytoskeletal and signaling proteins
    • Sheng, M., and Pak, D. T. (2000) Ligand-gated ion channel interactions with cytoskeletal and signaling proteins. Annu. Rev. Physiol. 62, 755-778
    • (2000) Annu. Rev. Physiol. , vol.62 , pp. 755-778
    • Sheng, M.1    Pak, D.T.2
  • 62
    • 0037013318 scopus 로고    scopus 로고
    • The PDZ proteins PICK1, GRIP, and syntenin bind multiple glutamate receptor subtypes. Analysis of PDZ binding motifs
    • Hirbec, H., Perestenko, O., Nishimune, A., Meyer, G., Nakanishi, S., Henley, J. M., and Dev, K. K. (2002) The PDZ proteins PICK1, GRIP, and syntenin bind multiple glutamate receptor subtypes. Analysis of PDZ binding motifs. J. Biol. Chem. 277, 15221-15224
    • (2002) J. Biol. Chem. , vol.277 , pp. 15221-15224
    • Hirbec, H.1    Perestenko, O.2    Nishimune, A.3    Meyer, G.4    Nakanishi, S.5    Henley, J.M.6    Dev, K.K.7
  • 63
    • 0030870335 scopus 로고    scopus 로고
    • Use of the two-hybrid system to find novel proteins that interact with alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) receptor subunits
    • Henley, J. M., Nishimune, A., Nash, S. R., and Nakanishi, S. (1997) Use of the two-hybrid system to find novel proteins that interact with alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) receptor subunits. Biochem. Soc. Trans. 25, 838-842
    • (1997) Biochem. Soc. Trans. , vol.25 , pp. 838-842
    • Henley, J.M.1    Nishimune, A.2    Nash, S.R.3    Nakanishi, S.4
  • 64
    • 0029946167 scopus 로고    scopus 로고
    • Interaction between the C-terminus of NMDA receptor subunits and multiple members of the PSD-95 family of membrane-associated guanylate kinases
    • Niethammer, M., Kim, E., and Sheng, M. (1996) Interaction between the C-terminus of NMDA receptor subunits and multiple members of the PSD-95 family of membrane-associated guanylate kinases. J. Neurosci. 16, 2157-2163
    • (1996) J. Neurosci. , vol.16 , pp. 2157-2163
    • Niethammer, M.1    Kim, E.2    Sheng, M.3
  • 65
    • 0032919444 scopus 로고    scopus 로고
    • Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy
    • Opella, S. J., Marassi, F. M., Gesell, J. J., Valente, A. P., Kim, Y., Oblatt-Montal, M., and Montal, M. (1999) Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy. Nat. Struct. Biol. 6, 374-379
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 374-379
    • Opella, S.J.1    Marassi, F.M.2    Gesell, J.J.3    Valente, A.P.4    Kim, Y.5    Oblatt-Montal, M.6    Montal, M.7
  • 66
    • 17144450204 scopus 로고    scopus 로고
    • Identification of the amino acid subsets accounting for the ligand binding specificity of a glutamate receptor
    • Paas, Y., Eisenstein, M., Medevielle, F., Teichberg, V. I., and Devillers-Thiery, A. (1996) Identification of the amino acid subsets accounting for the ligand binding specificity of a glutamate receptor. Neuron 17, 979-990
    • (1996) Neuron , vol.17 , pp. 979-990
    • Paas, Y.1    Eisenstein, M.2    Medevielle, F.3    Teichberg, V.I.4    Devillers-Thiery, A.5
  • 68
    • 0002449713 scopus 로고    scopus 로고
    • How well can molecular modelling predict the crystal structure: The case of the ligand-binding domain of glutamate receptors
    • Paas, Y., Devillers-Thiery, A., Teichberg, V. I., Changeux, J. P., and Eisenstein, M. (2000) How well can molecular modelling predict the crystal structure: the case of the ligand-binding domain of glutamate receptors. Trends Pharmacol. Sci. 21, 87-92
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 87-92
    • Paas, Y.1    Devillers-Thiery, A.2    Teichberg, V.I.3    Changeux, J.P.4    Eisenstein, M.5
  • 69
    • 0029583151 scopus 로고
    • Molecular dissection of the agonist binding site of an AMPA receptor
    • Kuusinen, A., Arvola, M., and Keinänen, K. (1995) Molecular dissection of the agonist binding site of an AMPA receptor. EMBO J. 14, 6327-6332
    • (1995) EMBO J. , vol.14 , pp. 6327-6332
    • Kuusinen, A.1    Arvola, M.2    Keinänen, K.3
  • 70
    • 0032521643 scopus 로고    scopus 로고
    • Characterization of the kainate-binding domain of the glutamate receptor GluR-6 subunit
    • Keinanen, K., Jouppila, A., and Kuusinen, A. (1998) Characterization of the kainate-binding domain of the glutamate receptor GluR-6 subunit. Biochem. J. 330, 1461-1467
    • (1998) Biochem. J. , vol.330 , pp. 1461-1467
    • Keinanen, K.1    Jouppila, A.2    Kuusinen, A.3
  • 71
    • 0031471216 scopus 로고    scopus 로고
    • Overexpression of a glutamate receptor (GluR2) ligand binding domain in Escherichia coli: Application of a novel protein folding screen
    • Chen, G. Q., and Gouaux, E. (1997) Overexpression of a glutamate receptor (GluR2) ligand binding domain in Escherichia coli: application of a novel protein folding screen. Proc. Natl. Acad. Sci. USA 94, 13431-13436
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13431-13436
    • Chen, G.Q.1    Gouaux, E.2
  • 72
    • 0030013631 scopus 로고    scopus 로고
    • Characterization of the ligand-binding domains of glutamate receptor (GluR)-B and GluR-D subunits expressed in Escherichia coli as periplasmic proteins
    • Arvola, M., and Keinänen, K. (1996) Characterization of the ligand-binding domains of glutamate receptor (GluR)-B and GluR-D subunits expressed in Escherichia coli as periplasmic proteins. J. Biol. Chem. 271, 15527-15532
    • (1996) J. Biol. Chem. , vol.271 , pp. 15527-15532
    • Arvola, M.1    Keinänen, K.2
  • 73
    • 0038719670 scopus 로고    scopus 로고
    • Is the isolated ligand binding domain a good model of the domain in the native receptor?
    • Deming, D., Cheng, Q., and Jayaraman, V. (2003) Is the isolated ligand binding domain a good model of the domain in the native receptor? J. Biol. Chem. 278, 17589-17592
    • (2003) J. Biol. Chem. , vol.278 , pp. 17589-17592
    • Deming, D.1    Cheng, Q.2    Jayaraman, V.3
  • 74
    • 0028811610 scopus 로고
    • Purification of recombinant GluR-D glutamate receptor produced in Sf21 insect cells
    • Kuusinen, A., Arvola, M., Oker-Blom, C., and Keinanen, K. (1995) Purification of recombinant GluR-D glutamate receptor produced in Sf21 insect cells. Eur. J. Biochem. 233, 720-726
    • (1995) Eur. J. Biochem. , vol.233 , pp. 720-726
    • Kuusinen, A.1    Arvola, M.2    Oker-Blom, C.3    Keinanen, K.4
  • 75
    • 0030799149 scopus 로고    scopus 로고
    • Ligand recognition in glutamate receptors: Insights from mutagenesis of the soluble alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-binding domain of glutamate receptor type D (GluR-D)
    • Keinanen, K., Arvola, M., Kuusinen, A., and Johnson, M. (1997) Ligand recognition in glutamate receptors: insights from mutagenesis of the soluble alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-binding domain of glutamate receptor type D (GluR-D). Biochem. Soc. Trans. 25, 835-838
    • (1997) Biochem. Soc. Trans. , vol.25 , pp. 835-838
    • Keinanen, K.1    Arvola, M.2    Kuusinen, A.3    Johnson, M.4
  • 76
    • 0030991790 scopus 로고    scopus 로고
    • Molecular determinants of agonist discrimination by NMDA receptor subunits: Analysis of the glutamate binding site on the NR2B subunit
    • Laube, B., Hirai, H., Sturgess, M., Betz, H., and Kuhse, J. (1997) Molecular determinants of agonist discrimination by NMDA receptor subunits: analysis of the glutamate binding site on the NR2B subunit. Neuron 18, 493-503
    • (1997) Neuron , vol.18 , pp. 493-503
    • Laube, B.1    Hirai, H.2    Sturgess, M.3    Betz, H.4    Kuhse, J.5
  • 77
    • 0033600566 scopus 로고    scopus 로고
    • A molecular envelope of the ligand-binding domain of a glutamate receptor in the presence and absence of agonist
    • Abele, R., Svergun, D., Keinanen, K., Koch, M. H., and Madden, D. R. (1999) A molecular envelope of the ligand-binding domain of a glutamate receptor in the presence and absence of agonist. Biochemistry 38, 10949-10957
    • (1999) Biochemistry , vol.38 , pp. 10949-10957
    • Abele, R.1    Svergun, D.2    Keinanen, K.3    Koch, M.H.4    Madden, D.R.5
  • 78
    • 0033947763 scopus 로고    scopus 로고
    • Large-scale expression and thermodynamic characterization of a glutamate receptor agonist-binding domain
    • Madden, D. R., Abele, R., Andersson, A., and Keinanen, K. (2000) Large-scale expression and thermodynamic characterization of a glutamate receptor agonist-binding domain. Eur. J. Biochem. 267, 4281-4289
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4281-4289
    • Madden, D.R.1    Abele, R.2    Andersson, A.3    Keinanen, K.4
  • 79
    • 0040355740 scopus 로고    scopus 로고
    • Agonist-induced isomerization in a glutamate receptor ligand-binding domain. A kinetic and mutagenetic analysis
    • Abele, R., Keinanen, K., and Madden, D. R. (2000) Agonist-induced isomerization in a glutamate receptor ligand-binding domain. A kinetic and mutagenetic analysis. J. Biol. Chem. 275, 21355-21363
    • (2000) J. Biol. Chem. , vol.275 , pp. 21355-21363
    • Abele, R.1    Keinanen, K.2    Madden, D.R.3
  • 80
    • 0035851125 scopus 로고    scopus 로고
    • Stereochemistry of quinoxaline antagonist binding to a glutamate receptor investigated by Fourier transform infrared spectroscopy
    • Madden, D. R., Thiran, S., Zimmermann, H., Romm, J., and Jayaraman, V. (2001) Stereochemistry of quinoxaline antagonist binding to a glutamate receptor investigated by Fourier transform infrared spectroscopy. J. Biol. Chem. 276, 37821-37826
    • (2001) J. Biol. Chem. , vol.276 , pp. 37821-37826
    • Madden, D.R.1    Thiran, S.2    Zimmermann, H.3    Romm, J.4    Jayaraman, V.5
  • 81
    • 0039592758 scopus 로고    scopus 로고
    • Ligand-protein interactions in the glutamate receptor
    • Jayaraman, V., Keesey, R., and Madden, D. R. (2000) Ligand-protein interactions in the glutamate receptor. Biochemistry 39, 8693-8697
    • (2000) Biochemistry , vol.39 , pp. 8693-8697
    • Jayaraman, V.1    Keesey, R.2    Madden, D.R.3
  • 82
    • 0037022201 scopus 로고    scopus 로고
    • A vibrational spectroscopic investigation of interactions of agonists with GluR0, a prokaryotic glutamate receptor
    • Cheng, Q., Thiran, S., Yernool, D., Gouaux, E., and Jayaraman, V. (2002) A vibrational spectroscopic investigation of interactions of agonists with GluR0, a prokaryotic glutamate receptor. Biochemistry 41, 1602-1608
    • (2002) Biochemistry , vol.41 , pp. 1602-1608
    • Cheng, Q.1    Thiran, S.2    Yernool, D.3    Gouaux, E.4    Jayaraman, V.5
  • 83
    • 0034602921 scopus 로고    scopus 로고
    • Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: Differences in solution and crystal forms of maltodextrin binding protein loaded with beta-cyclodextrin
    • Skrynnikov, N. R., Goto, N. K., Yang, D., Choy, W. Y., Tolman, J. R., Mueller, G. A., and Kay, L. E. (2000) Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: differences in solution and crystal forms of maltodextrin binding protein loaded with beta-cyclodextrin. J. Mol. Biol. 295, 1265-1273
    • (2000) J. Mol. Biol. , vol.295 , pp. 1265-1273
    • Skrynnikov, N.R.1    Goto, N.K.2    Yang, D.3    Choy, W.Y.4    Tolman, J.R.5    Mueller, G.A.6    Kay, L.E.7
  • 84
    • 0034972906 scopus 로고    scopus 로고
    • What is the average conformation of bacteriophage T4 lysozyme in solution? A domain orientation study using dipolar couplings measured by solution NMR
    • Goto, N. K., Skrynnikov, N. R., Dahlquist, F. W., and Kay, L. E. (2001) What is the average conformation of bacteriophage T4 lysozyme in solution? A domain orientation study using dipolar couplings measured by solution NMR. J. Mol. Biol. 308, 745-764
    • (2001) J. Mol. Biol. , vol.308 , pp. 745-764
    • Goto, N.K.1    Skrynnikov, N.R.2    Dahlquist, F.W.3    Kay, L.E.4
  • 85
    • 0037195266 scopus 로고    scopus 로고
    • Detecting protein kinase recognition modes of calmodulin by residual dipolar couplings in solution NMR
    • Mal, T. K., Skrynnikov, N. R., Yap, K. L., Kay, L. E., and Ikura, M. (2002) Detecting protein kinase recognition modes of calmodulin by residual dipolar couplings in solution NMR. Biochemistry 41, 12899-12906
    • (2002) Biochemistry , vol.41 , pp. 12899-12906
    • Mal, T.K.1    Skrynnikov, N.R.2    Yap, K.L.3    Kay, L.E.4    Ikura, M.5
  • 86
    • 0035003258 scopus 로고    scopus 로고
    • Structural similarities between glutamate receptor channels and K(+) channels examined by scanning mutagenesis
    • Panchenko, V. A., Glasser, C. R., and Mayer, M. L. (2001) Structural similarities between glutamate receptor channels and K(+) channels examined by scanning mutagenesis. J. Gen. Physiol. 117, 345-360
    • (2001) J. Gen. Physiol. , vol.117 , pp. 345-360
    • Panchenko, V.A.1    Glasser, C.R.2    Mayer, M.L.3
  • 87
    • 0037088901 scopus 로고    scopus 로고
    • The NMDA receptor M3 segment is a conserved transduction element coupling ligand binding to channel opening
    • Jones, K. S., VanDongen, H. M., and VanDongen, A. M. (2002) The NMDA receptor M3 segment is a conserved transduction element coupling ligand binding to channel opening. J. Neurosci. 22, 2044-2053
    • (2002) J. Neurosci. , vol.22 , pp. 2044-2053
    • Jones, K.S.1    VanDongen, H.M.2    VanDongen, A.M.3
  • 88
    • 0029071823 scopus 로고
    • Structural conservation of ion conduction pathways in K channels and glutamate receptors
    • Wood, M. W., Van Dongen, H. M. A., and Van Dongen, A. M. J. (1995) Structural conservation of ion conduction pathways in K channels and glutamate receptors. Proc. Natl. Acad. Sci. USA 92, 4882-4886
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4882-4886
    • Wood, M.W.1    Van Dongen, H.M.A.2    Van Dongen, A.M.J.3
  • 89
    • 0033516590 scopus 로고    scopus 로고
    • The cavity and pore helices in the KcsA K+ channel: Electrostatic stabilization of monovalent cations
    • Roux, B., and MacKinnon, R. (1999) The cavity and pore helices in the KcsA K+ channel: electrostatic stabilization of monovalent cations. Science 285, 100-102
    • (1999) Science , vol.285 , pp. 100-102
    • Roux, B.1    MacKinnon, R.2
  • 90
    • 0031015614 scopus 로고    scopus 로고
    • Single-channel properties of recombinant AMPA receptors depend on RNA editing, splice variation, and subunit composition
    • Swanson, G. T., Kamboj, S. K., and Cull-Candy, S. G. (1997) Single-channel properties of recombinant AMPA receptors depend on RNA editing, splice variation, and subunit composition. J. Neurosci. 17, 58-69
    • (1997) J. Neurosci. , vol.17 , pp. 58-69
    • Swanson, G.T.1    Kamboj, S.K.2    Cull-Candy, S.G.3
  • 92
    • 0043033172 scopus 로고    scopus 로고
    • Structural basis for partial agonist action at ionotropic glutamate receptors
    • Jin, R., Banke, T. G., Mayer, M. L., Traynelis, S. F., and Gouaux, E. (2003) Structural basis for partial agonist action at ionotropic glutamate receptors. Nat. Neurosci. 6, 803-810
    • (2003) Nat. Neurosci. , vol.6 , pp. 803-810
    • Jin, R.1    Banke, T.G.2    Mayer, M.L.3    Traynelis, S.F.4    Gouaux, E.5
  • 94
    • 0028106033 scopus 로고
    • The histidine-binding protein undergoes conformational changes in the absence of ligand as analyzed with conformation-specific monoclonal antibodies
    • Wolf, A., Shaw, E. W., Nikaido, K., and Ames, G. F. (1994) The histidine-binding protein undergoes conformational changes in the absence of ligand as analyzed with conformation-specific monoclonal antibodies. J. Biol. Chem. 269, 23051-23058
    • (1994) J. Biol. Chem. , vol.269 , pp. 23051-23058
    • Wolf, A.1    Shaw, E.W.2    Nikaido, K.3    Ames, G.F.4
  • 95
    • 0028929925 scopus 로고
    • Large amplitude twisting motions of an interdomain hinge: A disulfide trapping study of the galactose-glucose binding protein
    • Careaga, C. L., Sutherland, J., Sabeti, J., and Falke, J. J. (1995) Large amplitude twisting motions of an interdomain hinge: a disulfide trapping study of the galactose-glucose binding protein. Biochemistry 34, 3048-3055
    • (1995) Biochemistry , vol.34 , pp. 3048-3055
    • Careaga, C.L.1    Sutherland, J.2    Sabeti, J.3    Falke, J.J.4
  • 96
    • 0034114521 scopus 로고    scopus 로고
    • Mutation of a glutamate receptor motif reveals its role in gating and delta2 receptor channel properties
    • Kohda, K., Wang, Y., and Yuzaki, M. (2000) Mutation of a glutamate receptor motif reveals its role in gating and delta2 receptor channel properties. Nat. Neurosci. 3, 315-322
    • (2000) Nat. Neurosci. , vol.3 , pp. 315-322
    • Kohda, K.1    Wang, Y.2    Yuzaki, M.3
  • 98
    • 0032142987 scopus 로고    scopus 로고
    • Calmodulin mediates calcium-dependent inactivation of N-methyl-D-aspartate receptors
    • Zhang, S., Ehlers, M. D., Bernhardt, J. P., Su, C. T., and Huganir, R. L. (1998) Calmodulin mediates calcium-dependent inactivation of N-methyl-D-aspartate receptors. Neuron 21, 443-453
    • (1998) Neuron , vol.21 , pp. 443-453
    • Zhang, S.1    Ehlers, M.D.2    Bernhardt, J.P.3    Su, C.T.4    Huganir, R.L.5
  • 99
    • 0036830592 scopus 로고    scopus 로고
    • Discrimination between agonists and antagonists by the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid-selective glutamate receptor. A mutation analysis of the ligand-binding domain of GluR-D subunit
    • Lampinen, M., Settimo, L., Pentikainen, O. T., Jouppila, A., Mottershead, D. G., Johnson, M. S., and Keinanen, K. (2002) Discrimination between agonists and antagonists by the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid-selective glutamate receptor. A mutation analysis of the ligand-binding domain of GluR-D subunit. J. Biol. Chem. 277, 41940-41947
    • (2002) J. Biol. Chem. , vol.277 , pp. 41940-41947
    • Lampinen, M.1    Settimo, L.2    Pentikainen, O.T.3    Jouppila, A.4    Mottershead, D.G.5    Johnson, M.S.6    Keinanen, K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.