메뉴 건너뛰기




Volumn 67, Issue 5, 2005, Pages 1470-1484

Structural features of the glutamate binding site in recombinant NR1/NR2A N-methyl-D-aspartate receptors determined by site-directed mutagenesis and molecular modeling

Author keywords

[No Author keywords available]

Indexed keywords

AMPA RECEPTOR AGONIST; ASPARTIC ACID; GLUTAMIC ACID; GLYCINE; METHANETHIOSULFONATE ETHYLAMMONIUM; N METHYL DEXTRO ASPARTIC ACID; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; N METHYL DEXTRO ASPARTIC ACID RECEPTOR 1; N METHYL DEXTRO ASPARTIC ACID RECEPTOR 2A; SULFONIC ACID DERIVATIVE; TETRAZOL 5 YL GLYCINE; UNCLASSIFIED DRUG;

EID: 17844387335     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: 10.1124/mol.104.008185     Document Type: Article
Times cited : (139)

References (41)
  • 1
    • 0031961764 scopus 로고    scopus 로고
    • Identification of amino acid residues of the NR2A subunit that control glutamate potency in recombinant NR1/NR2A NMDA receptors
    • Anson LC, Chen PE, Wyllie DJA, Colquhoun D, and Schoepfer R (1998) Identification of amino acid residues of the NR2A subunit that control glutamate potency in recombinant NR1/NR2A NMDA receptors. J Neurosci 18:581-589.
    • (1998) J Neurosci , vol.18 , pp. 581-589
    • Anson, L.C.1    Chen, P.E.2    Wyllie, D.J.A.3    Colquhoun, D.4    Schoepfer, R.5
  • 2
    • 0034283106 scopus 로고    scopus 로고
    • Single-channel analysis of a NMDA receptor possessing a mutation in the region of the glutamate binding site
    • Anson LC, Schoepfer R, Colquhoun D, and Wyllie DJA (2000) Single-channel analysis of a NMDA receptor possessing a mutation in the region of the glutamate binding site. J Physiol (Lond) 527:225-237.
    • (2000) J Physiol (Lond) , vol.527 , pp. 225-237
    • Anson, L.C.1    Schoepfer, R.2    Colquhoun, D.3    Wyllie, D.J.A.4
  • 3
    • 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
  • 4
    • 0032578635 scopus 로고    scopus 로고
    • Structure of a glutamate-receptor ligand-binding core in complex with kainate
    • Armstrong N, Sun Y, Chen GQ, and Gouaux E (1998) Structure of a glutamate-receptor ligand-binding core in complex with kainate. Nature (Lond) 395:913-917.
    • (1998) Nature (Lond) , vol.395 , pp. 913-917
    • Armstrong, N.1    Sun, Y.2    Chen, G.Q.3    Gouaux, E.4
  • 5
    • 0025082936 scopus 로고
    • A kinetic analysis of the modulation of N-methyl-D-aspartic acid receptors by glycine in mouse cultured hippocampal neurones
    • Benveniste M, Clements J, Vyklicky L Jr, and Mayer ML (1990) A kinetic analysis of the modulation of N-methyl-D-aspartic acid receptors by glycine in mouse cultured hippocampal neurones. J Physiol (Lond) 428:333-357.
    • (1990) J Physiol (Lond) , vol.428 , pp. 333-357
    • Benveniste, M.1    Clements, J.2    Vyklicky Jr., L.3    Mayer, M.L.4
  • 6
    • 0033576612 scopus 로고    scopus 로고
    • Functional characterization of a potassium-selective prokaryotic glutamate receptor
    • Chen GQ, Cui C, Mayer ML, and Gouaux E (1999) Functional characterization of a potassium-selective prokaryotic glutamate receptor. Nature (Lond) 402:817-821.
    • (1999) Nature (Lond) , vol.402 , pp. 817-821
    • Chen, G.Q.1    Cui, C.2    Mayer, M.L.3    Gouaux, E.4
  • 7
    • 4043131606 scopus 로고    scopus 로고
    • Influence of a threonine residue in the S2 ligand binding domain in determining agonist potency and deactivation rate of recombinant NR1a/NR2D NMDA receptors
    • Chen PE, Johnston AR, Mok MHS, Schoepfer R, and Wyllie DJA (2004) Influence of a threonine residue in the S2 ligand binding domain in determining agonist potency and deactivation rate of recombinant NR1a/NR2D NMDA receptors. J Physiol (Lond) 558:45-58.
    • (2004) J Physiol (Lond) , vol.558 , pp. 45-58
    • Chen, P.E.1    Johnston, A.R.2    Mok, M.H.S.3    Schoepfer, R.4    Wyllie, D.J.A.5
  • 8
    • 0008151665 scopus 로고    scopus 로고
    • Structural insights into NMDA ionotropic glutamate receptors via molecular modeling
    • Chohan KK, Wo ZG, Oswald RE, and Sutcliffe MJ (2000) Structural insights into NMDA ionotropic glutamate receptors via molecular modeling. J Mol Model (Online) 6:16-25.
    • (2000) J Mol Model (Online) , vol.6 , pp. 16-25
    • Chohan, K.K.1    Wo, Z.G.2    Oswald, R.E.3    Sutcliffe, M.J.4
  • 9
    • 0032199006 scopus 로고    scopus 로고
    • Binding, gating, affinity and efficacy: The interpretation of structure-activity relationships for agonists and of the effects of mutating receptors
    • Colquhoun D (1998) Binding, gating, affinity and efficacy: the interpretation of structure-activity relationships for agonists and of the effects of mutating receptors. Br J Pharmacol 125:924-947.
    • (1998) Br J Pharmacol , vol.125 , pp. 924-947
    • Colquhoun, D.1
  • 11
    • 0030043489 scopus 로고    scopus 로고
    • Cation-π interactions in chemistry and biology: A new view of benzene, Phe, Tyr and Trp
    • Dougherty DA (1996) Cation-π interactions in chemistry and biology: a new view of benzene, Phe, Tyr and Trp. Science (Wash DC) 271:163-168.
    • (1996) Science (Wash DC) , vol.271 , pp. 163-168
    • Dougherty, D.A.1
  • 13
    • 14944364531 scopus 로고    scopus 로고
    • Subunit-specific gating controls rat NR1/NR2A and NR1/NR2B NMDA channel kinetics and synaptic signaling profiles
    • Erreger K, Dravid SM, Banke TG, Wyllie DJA, and Traynelis SF (2005) Subunit-specific gating controls rat NR1/NR2A and NR1/NR2B NMDA channel kinetics and synaptic signaling profiles. J Physiol (Lond) 563:345-358.
    • (2005) J Physiol (Lond) , vol.563 , pp. 345-358
    • Erreger, K.1    Dravid, S.M.2    Banke, T.G.3    Wyllie, D.J.A.4    Traynelis, S.F.5
  • 14
    • 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 (Eur Mol Biol Organ) J 22:2873-2885.
    • (2003) EMBO (Eur Mol Biol Organ) J , vol.22 , pp. 2873-2885
    • Furukawa, H.1    Gouaux, E.2
  • 15
    • 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 JS, Jin R, Liljefors T, Mayer ML, Egebjerg J, Larsen IK, 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.S.2    Jin, R.3    Liljefors, T.4    Mayer, M.L.5    Egebjerg, J.6    Larsen, I.K.7    Gouaux, E.8
  • 16
    • 0027197230 scopus 로고
    • Zinc potentiates agonist-induced currents at certain splice variants of the NMDA receptor
    • Hollmann M, Boulter J, Maron C, Beasley L, Sullivan J, Pecht G, and Heinemann S (1993) Zinc potentiates agonist-induced currents at certain splice variants of the NMDA receptor. Neuron 10:943-954.
    • (1993) Neuron , vol.10 , pp. 943-954
    • Hollmann, M.1    Boulter, J.2    Maron, C.3    Beasley, L.4    Sullivan, J.5    Pecht, G.6    Heinemann, S.7
  • 17
    • 0037088901 scopus 로고    scopus 로고
    • The NMDA receptor M3 segment is a conserved transduction element coupling ligand binding to channel opening
    • Jones KS, VanDongen HM, and VanDongen AM (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
  • 18
    • 3342967463 scopus 로고    scopus 로고
    • Ligand-binding residues integrate affinity and efficacy in the NMDA receptor
    • Kalbaugh TL, VanDongen HMA, and VanDongen AMJ (2004) Ligand-binding residues integrate affinity and efficacy in the NMDA receptor. Mol Pharmacol 66:209-219.
    • (2004) Mol Pharmacol , vol.66 , pp. 209-219
    • Kalbaugh, T.L.1    VanDongen, H.M.A.2    VanDongen, A.M.J.3
  • 19
    • 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 ML, Liljefors T, Gouaux E, Egebjerg J, and Kastrup JS (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
  • 20
    • 0030000465 scopus 로고    scopus 로고
    • 2+ block in NMDA receptor channels
    • 2+ block in NMDA receptor channels. J Neurosci 16:3549-3558.
    • (1996) J Neurosci , vol.16 , pp. 3549-3558
    • Kuner, T.1    Schoepfer, R.2
  • 21
    • 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, and 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
  • 22
    • 0029583151 scopus 로고
    • Molecular dissection of the agonist binding site of an AMPA receptor
    • Kuusinen A, Arvola M, and Keinanen K (1995) Molecular dissection of the agonist binding site of an AMPA receptor. EMBO (Eur Mol Biol Organ) J 14:6327-6332.
    • (1995) EMBO (Eur Mol Biol Organ) J , vol.14 , pp. 6327-6332
    • Kuusinen, A.1    Arvola, M.2    Keinanen, K.3
  • 23
    • 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
  • 24
    • 8844247179 scopus 로고    scopus 로고
    • Molecular determinants of ligand discrimination in the glutamate-binding pocket of the NMDA receptor
    • Laube B, Schemm R, and Betz B (2004) Molecular determinants of ligand discrimination in the glutamate-binding pocket of the NMDA receptor. Neuropharmacology 47:994-1007.
    • (2004) Neuropharmacology , vol.47 , pp. 994-1007
    • Laube, B.1    Schemm, R.2    Betz, B.3
  • 25
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl E, Hess B, and van der Spoel D (2001) GROMACS 3.0: a package for molecular simulation and trajectory analysis. J Mol Model (Online) 7:306-317.
    • (2001) J Mol Model (Online) , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 26
    • 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 ML, Hogner A, Stensbol TB, Gouaux E, Egebjerg J, and Kastrup JS (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
  • 27
    • 4243468938 scopus 로고    scopus 로고
    • The cation-π interaction
    • Ma JC and Dougherty DA (1997) The cation-π interaction. Chem Rev 5:1303-1324.
    • (1997) Chem Rev , vol.5 , pp. 1303-1324
    • Ma, J.C.1    Dougherty, D.A.2
  • 28
    • 0028343648 scopus 로고
    • Developmental and regional expression in the rat brain and functional properties of four NMDA receptors
    • Monyer H, Burnashev N, Laurie DJ, Sakmann B, and Seeburg PH (1994) Developmental and regional expression in the rat brain and functional properties of four NMDA receptors. Neuron 12:529-540.
    • (1994) Neuron , vol.12 , pp. 529-540
    • Monyer, H.1    Burnashev, N.2    Laurie, D.J.3    Sakmann, B.4    Seeburg, P.H.5
  • 30
    • 0028067178 scopus 로고
    • The bacterial periplasmic histidine-binding protein. Structure/function analysis of the ligand-binding site and comparison with related proteins
    • Oh BH, Rang CH, De Bondt H, Kim SH, Nikaido K, Joshl AK, and Ames GF (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.
    • (1994) J Biol Chem , vol.269 , pp. 4135-4143
    • Oh, B.H.1    Rang, C.H.2    De Bondt, H.3    Kim, S.H.4    Nikaido, K.5    Joshl, A.K.6    Ames, G.F.7
  • 31
    • 0027235488 scopus 로고
    • Three-dimensional structures of the periplasmic lysine/arginine/ ornithine-binding protein with and without a ligand
    • Oh BH, Pandit J, Kang CH, Nikaido K, Gokcen S, Ames GF, and Kim SH (1993) Three-dimensional structures of the periplasmic lysine/arginine/ornithine- binding protein with and without a ligand. J Biol Chem 268:11348-11355.
    • (1993) J Biol Chem , vol.268 , pp. 11348-11355
    • Oh, B.H.1    Pandit, J.2    Kang, C.H.3    Nikaido, K.4    Gokcen, S.5    Ames, G.F.6    Kim, S.H.7
  • 32
    • 0032032919 scopus 로고    scopus 로고
    • The macro- and microarchitectures of the ligand-binding domain of glutamate receptors
    • Paas Y (1998) The macro- and microarchitectures of the ligand-binding domain of glutamate receptors. Trends Neurosci 21:117-125.
    • (1998) Trends Neurosci , vol.21 , pp. 117-125
    • Paas, Y.1
  • 33
    • 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 VI, 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
  • 35
    • 0037442813 scopus 로고    scopus 로고
    • Studies of NMDA receptor function and stoichiometry with truncated and tandem subunits
    • Schorge S and Colquhoun D (2003) Studies of NMDA receptor function and stoichiometry with truncated and tandem subunits. J Neurosci 23:1151-1158.
    • (2003) J Neurosci , vol.23 , pp. 1151-1158
    • Schorge, S.1    Colquhoun, D.2
  • 36
    • 84962377223 scopus 로고    scopus 로고
    • 3-Fluoropiperidines and N-methyl-3-fluoropiperidinium salts: The persistence of axial fluorine
    • Sun A, Lankin DC, Hardcastle K, and Snyder JP (2005) 3-Fluoropiperidines and N-methyl-3-fluoropiperidinium salts: the persistence of axial fluorine. Chem Eur J 11:1579-1591.
    • (2005) Chem Eur J , vol.11 , pp. 1579-1591
    • Sun, A.1    Lankin, D.C.2    Hardcastle, K.3    Snyder, J.P.4
  • 37
    • 0037194828 scopus 로고    scopus 로고
    • Structural basis for understanding structure-activity relationships for the glutamate binding site of the NMDA receptor
    • Tikhonova IG, Baskin II, Palyulin VA, Zefirov NS, and Bachurin SO (2002) Structural basis for understanding structure-activity relationships for the glutamate binding site of the NMDA receptor. J Biol Chem 18:3836-3843.
    • (2002) J Biol Chem , vol.18 , pp. 3836-3843
    • Tikhonova, I.G.1    Baskin, I.I.2    Palyulin, V.A.3    Zefirov, N.S.4    Bachurin, S.O.5
  • 39
    • 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, and 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
  • 40
    • 0033601326 scopus 로고    scopus 로고
    • Cysteine mutagenesis and homology modeling of the ligand-binding site of a kainate-binding protein
    • Wo ZG, Chohan KK, Chen H, Sutcliffe MJ, and Oswald RE (1999) Cysteine mutagenesis and homology modeling of the ligand-binding site of a kainate-binding protein. J Biol Chem 274:37210-37218.
    • (1999) J Biol Chem , vol.274 , pp. 37210-37218
    • Wo, Z.G.1    Chohan, K.K.2    Chen, H.3    Sutcliffe, M.J.4    Oswald, R.E.5
  • 41
    • 0001823013 scopus 로고    scopus 로고
    • Single-channel activations and concentration jumps: Comparison of recombinant NR1a/NR2A and NR1a/NR2D NMDA receptors
    • Wyllie DJA, Béhé P, and Colquhoun D (1998) Single-channel activations and concentration jumps: comparison of recombinant NR1a/NR2A and NR1a/NR2D NMDA receptors. J Physiol (Lond) 510:1-18.
    • (1998) J Physiol (Lond) , vol.510 , pp. 1-18
    • Wyllie, D.J.A.1    Béhé, P.2    Colquhoun, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.