메뉴 건너뛰기




Volumn 269, Issue 24, 2002, Pages 6261-6270

Determinants of antagonist binding at the α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor subunit, gluR-D: Role of the conserved arginine 507 and glutamate 727 residues

Author keywords

AMPA; Ionotropic glutamate receptor; Molecular modelling; Radioligand binding; Ro 48 8587

Indexed keywords

7,7 DINITROQUINOXALINE 2,3 DIONE; ALPHA AMINO 3 HYDROXY 5 METHYL 4 ISOXAZOLEPROPIONIC ACID; AMPA RECEPTOR; GLUTAMATE RECEPTOR; QUINOXALINE DERIVATIVE; RADIOLIGAND; RECEPTOR SUBUNIT; UNCLASSIFIED DRUG;

EID: 18744394305     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.03345.x     Document Type: Article
Times cited : (6)

References (37)
  • 3
    • 0036483593 scopus 로고    scopus 로고
    • The structure and function of glutamate receptor ion channels
    • Madden, D.R. (2002) The structure and function of glutamate receptor ion channels. Nature Rev. Neurosci. 3, 91-101.
    • (2002) Nature Rev. Neurosci. , vol.3 , pp. 91-101
    • Madden, D.R.1
  • 4
    • 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. & 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
  • 5
    • 0028284469 scopus 로고
    • Mutational analysis of the glycine-binding site of the NMDA receptor: Structural similarity with bacterial amino acid-binding proteins
    • Kuryatov, A., Laube, B., Betz, H. & Kuhse, J. (1994) Mutational analysis of the glycine-binding site of the NMDA receptor: Structural similarity with bacterial amino acid-binding proteins. Neuron 12, 1291-1300.
    • (1994) Neuron , vol.12 , pp. 1291-1300
    • Kuryatov, A.1    Laube, B.2    Betz, H.3    Kuhse, J.4
  • 6
    • 0029583151 scopus 로고
    • Molecular dissection of the agonist binding site of an AMPA receptor
    • Kuusinen, A., Arvola, M. & 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
  • 7
    • 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. & 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
  • 8
    • 0032578635 scopus 로고    scopus 로고
    • Structure of a glutamate-receptor ligand-binding core in complex with kainate
    • Armstrong, N., Sun, Y., Chen, G.Q. & Gouaux, E. (1998) Structure of a glutamate-receptor ligand-binding core in complex with kainate. Nature 395, 913-917.
    • (1998) Nature , vol.395 , pp. 913-917
    • Armstrong, N.1    Sun, Y.2    Chen, G.Q.3    Gouaux, E.4
  • 9
    • 0033636314 scopus 로고    scopus 로고
    • Mechanism for activation and antagonism of an AMPA-sensitive glutamate receptor: Crystal structures of the GluR2 ligand binding core
    • Armstrong, N. & Gouaux, E. (2000) Mechanism 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
  • 10
    • 0032541434 scopus 로고    scopus 로고
    • AMPA receptors and bacterial periplasmic amino acid-binding proteins share the ionic mechanism of ligand recognition
    • Lampinen, M., Pentikäinen, O., Johnson, M.S. & Keinänen, 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    Pentikäinen, O.2    Johnson, M.S.3    Keinänen, K.4
  • 11
    • 0029122075 scopus 로고
    • Synthesis of 1,4,7,8,9,10-hexahydro-9-methyl-6-nitropyrido[3,4-f]-quinoxaline-2,3-dione and related quinoxalinediones: Characterization of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (and N-methyl-D-aspartate) receptor and anticonvulsant activity
    • Bigge, C.F., Malone, T.C., Boxer, P.A., Nelson, C.B., Ortwine, D.F., Schelkun, R.M., Retz, D.M., Lescosky, L.J., Borosky, S.A., Vartanian, M.G., Schwarz, R.D., Campbell, G.W., Robichaud, L.J. & Wätjen, F. (1995) Synthesis of 1,4,7,8,9,10-hexahydro-9-methyl-6-nitropyrido[3,4-f]-quinoxaline-2,3-dione and related quinoxalinediones: Characterization of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (and N-methyl-D-aspartate) receptor and anticonvulsant activity. J. Med. Chem. 38, 3720-3740.
    • (1995) J. Med. Chem. , vol.38 , pp. 3720-3740
    • Bigge, C.F.1    Malone, T.C.2    Boxer, P.A.3    Nelson, C.B.4    Ortwine, D.F.5    Schelkun, R.M.6    Retz, D.M.7    Lescosky, L.J.8    Borosky, S.A.9    Vartanian, M.G.10    Schwarz, R.D.11    Campbell, G.W.12    Robichaud, L.J.13    Wätjen, F.14
  • 15
    • 0029101866 scopus 로고
    • 3H]NS 257, a novel competitive AMPA receptor antagonist, to rat brain membranes and brain sections
    • 3H]NS 257, a novel competitive AMPA receptor antagonist, to rat brain membranes and brain sections. J. Neurochem. 65, 1264-1273.
    • (1995) J. Neurochem. , vol.65 , pp. 1264-1273
    • Nielsen, E.O.1    Johansen, T.H.2    Watjen, F.3    Drejer, J.4
  • 18
    • 0032878510 scopus 로고    scopus 로고
    • Oligomerization and ligand-binding properties of the ectodomain of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor subunit GluRD
    • Kuusinen, A., Abele, R., Madden, D.R. & Keinänen, K. (1999) Oligomerization and ligand-binding properties of the ectodomain of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic 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    Keinänen, K.4
  • 19
    • 0028811610 scopus 로고
    • Purification of recombinant GluR-D glutamate receptor produced in Sf21 insect cells
    • Kuusinen, A., Arvola, M., Oker-Blom, C. & Keinänen, 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    Keinänen, K.4
  • 21
    • 0027361123 scopus 로고
    • A structural basis for sequence comparisons. An evaluation of scoring methodologies
    • Johnson, M.S. & Overington, J.P. (1993) A structural basis for sequence comparisons. An evaluation of scoring methodologies. J. Mol. Biol. 233, 716-738.
    • (1993) J. Mol. Biol. , vol.233 , pp. 716-738
    • Johnson, M.S.1    Overington, J.P.2
  • 22
    • 0029884429 scopus 로고    scopus 로고
    • Discrimination of common protein folds: Application of protein structure to sequence/structure comparisons
    • Johnson, M.S., May, A.C., Rodionov, M.A. & Overington, J.P. (1996) Discrimination of common protein folds: Application of protein structure to sequence/structure comparisons. Methods Enzymol. 266, 575-598.
    • (1996) Methods Enzymol. , vol.266 , pp. 575-598
    • Johnson, M.S.1    May, A.C.2    Rodionov, M.A.3    Overington, J.P.4
  • 23
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A. & Blundell, T.L. (1993) Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Šali, A.1    Blundell, T.L.2
  • 25
    • 84988053694 scopus 로고
    • An all atom force field for simulations of proteins and nucleic acids
    • Weiner, S.J., Kollman, P.A., Nguyen, D.T. & Case, D.A. (1986) An all atom force field for simulations of proteins and nucleic acids. J. Comput. Chem. 7, 230-252.
    • (1986) J. Comput. Chem. , vol.7 , pp. 230-252
    • Weiner, S.J.1    Kollman, P.A.2    Nguyen, D.T.3    Case, D.A.4
  • 27
  • 28
    • 0011134241 scopus 로고    scopus 로고
    • Merck molecular force field. II. MMFF94 van der Waals and electrostatic parameters for intermolecular interactions
    • Halgren, T.A. (1996) Merck molecular force field. II. MMFF94 van der Waals and electrostatic parameters for intermolecular interactions. J. Comput. Chem. 17, 520-552.
    • (1996) J. Comput. Chem. , vol.17 , pp. 520-552
    • Halgren, T.A.1
  • 31
    • 0036830592 scopus 로고    scopus 로고
    • Discrimination between agonists and antagonists by the a-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., Pentikäinen, O.T., Jouppila, A., Mottershead, D.G., Johnson, M. & Keinänen, K. (2002) Discrimination between agonists and antagonists by the a-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    Pentikäinen, O.T.3    Jouppila, A.4    Mottershead, D.G.5    Johnson, M.6    Keinänen, K.7
  • 32
    • 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. & 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
  • 34
    • 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. & 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
  • 35
    • 0040355740 scopus 로고    scopus 로고
    • Agonist-induced isomerization in a glutamate receptor ligand-binding domain. A kinetic and mutagenetic analysis
    • Abele, R., Keinänen, K. & Madden, D.R. (2000) Agonist-induced isomerization in a glutamate receptor ligand-binding domain. A kinetic and mutagenetic analysis. J. Biol. Chem. 28, 21355-21363.
    • (2000) J. Biol. Chem. , vol.28 , pp. 21355-21363
    • Abele, R.1    Keinänen, K.2    Madden, D.R.3
  • 36
    • 0029899637 scopus 로고    scopus 로고
    • A venus flytrap mechanism for activation and desensitization of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors
    • Mano, I., Lamed, Y. & Teichberg, V.I. (1996) A venus flytrap mechanism for activation and desensitization of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors. J. Biol. Chem. 271, 15299-15302.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15299-15302
    • Mano, I.1    Lamed, Y.2    Teichberg, V.I.3
  • 37
    • 0029921964 scopus 로고    scopus 로고
    • Activation of N-methyl-D-aspartate receptors by glycine: Role of an aspartate residue in the M3-M4 loop of the NR1 subunit
    • Williams, K., Chao, J., Kashiwagi, K., Masuko, T. & Igarashi, K. (1996) Activation of N-methyl-D-aspartate receptors by glycine: Role of an aspartate residue in the M3-M4 loop of the NR1 subunit. Mol. Pharmacol. 50, 701-708.
    • (1996) Mol. Pharmacol. , vol.50 , pp. 701-708
    • Williams, K.1    Chao, J.2    Kashiwagi, K.3    Masuko, T.4    Igarashi, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.