메뉴 건너뛰기




Volumn 57, Issue 2, 2009, Pages 127-136

The selectivity of conantokin-G for ion channel inhibition of NR2B subunit-containing NMDA receptors is regulated by amino acid residues in the S2 region of NR2B

Author keywords

Conantokins; Electrophysiology; Ion channels; NMDAR mutagenesis; NMDAR subtypes

Indexed keywords

AMINO ACID; CONANTOKIN G; ION CHANNEL; LYSINE; N METHYL DEXTRO ASPARTIC ACID RECEPTOR 2A; N METHYL DEXTRO ASPARTIC ACID RECEPTOR 2B; TYROSINE;

EID: 67650125196     PISSN: 00283908     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuropharm.2009.04.014     Document Type: Article
Times cited : (15)

References (38)
  • 1
    • 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. Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core. Neuron 28 (2000) 165-181
    • (2000) Neuron , vol.28 , pp. 165-181
    • Armstrong, N.1    Gouaux, E.2
  • 2
    • 2342649960 scopus 로고    scopus 로고
    • The effect of CGX-1007 and CI-1041, novel NMDA receptor antagonists, on NMDA receptor-mediated EPSCs
    • Barton M.E., White H.S., and Wilcox K.S. The effect of CGX-1007 and CI-1041, novel NMDA receptor antagonists, on NMDA receptor-mediated EPSCs. Epilepsy Res. 59 (2004) 13-24
    • (2004) Epilepsy Res. , vol.59 , pp. 13-24
    • Barton, M.E.1    White, H.S.2    Wilcox, K.S.3
  • 4
    • 57049105073 scopus 로고    scopus 로고
    • Voltage-dependent gating of NR1/2B NMDA receptors
    • Clarke R.J., and Johnson J.W. Voltage-dependent gating of NR1/2B NMDA receptors. J. Physiol. 586 (2008) 5727-5741
    • (2008) J. Physiol. , vol.586 , pp. 5727-5741
    • Clarke, R.J.1    Johnson, J.W.2
  • 5
    • 0033851790 scopus 로고    scopus 로고
    • Conantokin G is an NR2B-selective competitive antagonist of N-methyl-d-aspartate receptors
    • Donevan S.D., and McCabe R.T. Conantokin G is an NR2B-selective competitive antagonist of N-methyl-d-aspartate receptors. Mol. Pharmacol. 58 (2000) 614-623
    • (2000) Mol. Pharmacol. , vol.58 , pp. 614-623
    • Donevan, S.D.1    McCabe, R.T.2
  • 7
    • 27744500994 scopus 로고    scopus 로고
    • Subunit arrangement and function in NMDA receptors
    • Furukawa H., Singh S.K., Mancusso R., and Gouaux E. Subunit arrangement and function in NMDA receptors. Nature 438 (2005) 185-192
    • (2005) Nature , vol.438 , pp. 185-192
    • Furukawa, H.1    Singh, S.K.2    Mancusso, R.3    Gouaux, E.4
  • 8
    • 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. Mechanisms of activation, inhibition and specificity: crystal structures of the NMDA receptor NR1 ligand-binding core. Embo J. 22 (2003) 2873-2885
    • (2003) Embo J. , vol.22 , pp. 2873-2885
    • Furukawa, H.1    Gouaux, E.2
  • 10
    • 0025241893 scopus 로고
    • Conantokin-T. A γ-carboxyglutamate-containing peptide with N-methyl-d-aspartate antagonist activity
    • Haack J.A., Rivier J., Parks T.N., Mena E.E., Cruz L.J., and Olivera B.M. Conantokin-T. A γ-carboxyglutamate-containing peptide with N-methyl-d-aspartate antagonist activity. J. Biol. Chem. 265 (1990) 6025-6029
    • (1990) J. Biol. Chem. , vol.265 , pp. 6025-6029
    • Haack, J.A.1    Rivier, J.2    Parks, T.N.3    Mena, E.E.4    Cruz, L.J.5    Olivera, B.M.6
  • 11
    • 0029893942 scopus 로고    scopus 로고
    • 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
    • Hirai H., Kirsch J., Laube B., Betz H., and Kuhse J. 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. U.S.A. 93 (1996) 6031-6036
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 6031-6036
    • Hirai, H.1    Kirsch, J.2    Laube, B.3    Betz, H.4    Kuhse, J.5
  • 12
    • 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. Zinc potentiates agonist-induced currents at certain splice variants of the NMDA receptor. Neuron 10 (1993) 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
  • 15
    • 0035920125 scopus 로고    scopus 로고
    • The amino acid residue at sequence position 5 in the conantokin peptides partially governs subunit-selective antagonism of recombinant N-methyl-d-aspartate receptors
    • Klein R.C., Prorok M., Galdzicki Z., and Castellino F.J. The amino acid residue at sequence position 5 in the conantokin peptides partially governs subunit-selective antagonism of recombinant N-methyl-d-aspartate receptors. J. Biol. Chem. 276 (2001) 26860-26867
    • (2001) J. Biol. Chem. , vol.276 , pp. 26860-26867
    • Klein, R.C.1    Prorok, M.2    Galdzicki, Z.3    Castellino, F.J.4
  • 16
    • 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. Mutational analysis of the glycine-binding site of the NMDA receptor: structural similarity with bacterial amino acid-binding proteins. Neuron 12 (1994) 1291-1300
    • (1994) Neuron , vol.12 , pp. 1291-1300
    • Kuryatov, A.1    Laube, B.2    Betz, H.3    Kuhse, J.4
  • 17
    • 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. Molecular determinants of agonist discrimination by NMDA receptor subunits: analysis of the glutamate binding site on the NR2B subunit. Neuron 18 (1997) 493-503
    • (1997) Neuron , vol.18 , pp. 493-503
    • Laube, B.1    Hirai, H.2    Sturgess, M.3    Betz, H.4    Kuhse, J.5
  • 18
    • 0037219288 scopus 로고    scopus 로고
    • Powerful antinociceptive effects of the cone snail venom-derived subtype-selective NMDA receptor antagonists conantokins G and T
    • Malmberg A.B., Gilbert H., McCabe R.T., and Basbaum A.I. Powerful antinociceptive effects of the cone snail venom-derived subtype-selective NMDA receptor antagonists conantokins G and T. Pain 101 (2003) 109-116
    • (2003) Pain , vol.101 , pp. 109-116
    • Malmberg, A.B.1    Gilbert, H.2    McCabe, R.T.3    Basbaum, A.I.4
  • 19
    • 0033051714 scopus 로고    scopus 로고
    • A regulatory domain (R1-R2) in the amino terminus of the N-methyl-d-aspartate receptor: effects of spermine, protons, and ifenprodil, and structural similarity to bacterial leucine/isoleucine/valine binding protein
    • Masuko T., Kashiwagi K., Kuno T., Nguyen N.D., Pahk A.J., Fukuchi J., Igarashi K., and Williams K. A regulatory domain (R1-R2) in the amino terminus of the N-methyl-d-aspartate receptor: effects of spermine, protons, and ifenprodil, and structural similarity to bacterial leucine/isoleucine/valine binding protein. Mol. Pharmacol. 55 (1999) 957-969
    • (1999) Mol. Pharmacol. , vol.55 , pp. 957-969
    • Masuko, T.1    Kashiwagi, K.2    Kuno, T.3    Nguyen, N.D.4    Pahk, A.J.5    Fukuchi, J.6    Igarashi, K.7    Williams, K.8
  • 20
    • 0242526137 scopus 로고    scopus 로고
    • Specific assembly with the NMDA receptor 3B subunit controls surface expression and calcium permeability of NMDA receptors
    • Matsuda K., Fletcher M., Kamiya Y., and Yuzaki M. Specific assembly with the NMDA receptor 3B subunit controls surface expression and calcium permeability of NMDA receptors. J. Neurosci. 23 (2003) 10064-10073
    • (2003) J. Neurosci. , vol.23 , pp. 10064-10073
    • Matsuda, K.1    Fletcher, M.2    Kamiya, Y.3    Yuzaki, M.4
  • 21
    • 0021341121 scopus 로고
    • Voltage-dependent block by Mg2+ of NMDA responses in spinal cord neurones
    • Mayer M.L., Westbrook G.L., and Guthrie P.B. Voltage-dependent block by Mg2+ of NMDA responses in spinal cord neurones. Nature 309 (1984) 261-263
    • (1984) Nature , vol.309 , pp. 261-263
    • Mayer, M.L.1    Westbrook, G.L.2    Guthrie, P.B.3
  • 22
  • 23
    • 0021260967 scopus 로고
    • Magnesium gates glutamate-activated channels in mouse central neurones
    • Nowak L., Bregestovski P., Ascher P., Herbet A., and Prochiantz A. Magnesium gates glutamate-activated channels in mouse central neurones. Nature 307 (1984) 462-465
    • (1984) Nature , vol.307 , pp. 462-465
    • Nowak, L.1    Bregestovski, P.2    Ascher, P.3    Herbet, A.4    Prochiantz, A.5
  • 24
    • 0037101607 scopus 로고    scopus 로고
    • Mapping the binding site of the neuroprotectant ifenprodil on NMDA receptors
    • Perin-Dureau F., Rachline J., Neyton J., and Paoletti P. Mapping the binding site of the neuroprotectant ifenprodil on NMDA receptors. J. Neurosci. 22 (2002) 5955-5965
    • (2002) J. Neurosci. , vol.22 , pp. 5955-5965
    • Perin-Dureau, F.1    Rachline, J.2    Neyton, J.3    Paoletti, P.4
  • 25
    • 34249010244 scopus 로고    scopus 로고
    • The molecular basis of conantokin antagonism of NMDA receptor function
    • Prorok M., and Castellino F.J. The molecular basis of conantokin antagonism of NMDA receptor function. Curr. Drug Targets 8 (2007) 633-642
    • (2007) Curr. Drug Targets , vol.8 , pp. 633-642
    • Prorok, M.1    Castellino, F.J.2
  • 26
    • 0030449042 scopus 로고    scopus 로고
    • Calcium binding properties of synthetic γ-carboxyglutamic acid containing marine cone snail "sleeper" peptides, conantokin-G and conantokin-T
    • Prorok M., Warder S.E., Blandl T., and Castellino F.J. Calcium binding properties of synthetic γ-carboxyglutamic acid containing marine cone snail "sleeper" peptides, conantokin-G and conantokin-T. Biochemistry 35 (1996) 16528-16534
    • (1996) Biochemistry , vol.35 , pp. 16528-16534
    • Prorok, M.1    Warder, S.E.2    Blandl, T.3    Castellino, F.J.4
  • 27
    • 0033546347 scopus 로고    scopus 로고
    • Specific coupling of NMDA receptor activation to nitric oxide neurotoxicity by PSD-95 protein
    • Sattler R., Xiong Z., Lu W.Y., Hafner M., MacDonald J.F., and Tymianski M. Specific coupling of NMDA receptor activation to nitric oxide neurotoxicity by PSD-95 protein. Science 284 (1999) 1845-1848
    • (1999) Science , vol.284 , pp. 1845-1848
    • Sattler, R.1    Xiong, Z.2    Lu, W.Y.3    Hafner, M.4    MacDonald, J.F.5    Tymianski, M.6
  • 28
    • 34547211472 scopus 로고    scopus 로고
    • Subtype-selective antagonism of N-methyl-d-aspartate receptor ion channels by synthetic conantokin peptides
    • Sheng Z., Dai Q., Prorok M., and Castellino F.J. Subtype-selective antagonism of N-methyl-d-aspartate receptor ion channels by synthetic conantokin peptides. Neuropharmacology 53 (2007) 145-156
    • (2007) Neuropharmacology , vol.53 , pp. 145-156
    • Sheng, Z.1    Dai, Q.2    Prorok, M.3    Castellino, F.J.4
  • 29
    • 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. Structures and properties of seven isoforms of the NMDA receptor generated by alternative splicing. Biochem. Biophys. Res. Commun. 185 (1992) 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
  • 31
    • 0347989461 scopus 로고    scopus 로고
    • Conus venoms: a rich source of novel ion channel-targeted peptides
    • Terlau H., and Olivera B.M. Conus venoms: a rich source of novel ion channel-targeted peptides. Physiol. Rev. 84 (2004) 41-68
    • (2004) Physiol. Rev. , vol.84 , pp. 41-68
    • Terlau, H.1    Olivera, B.M.2
  • 32
    • 0031040615 scopus 로고    scopus 로고
    • Characterization of protein kinase A and protein kinase C phosphorylation of the N-methyl-d-aspartate receptor NR1 subunit using phosphorylation site-specific antibodies
    • Tingley W.G., Ehlers M.D., Kameyama K., Doherty C., Ptak J.B., Riley C.T., and Huganir R.L. Characterization of protein kinase A and protein kinase C phosphorylation of the N-methyl-d-aspartate receptor NR1 subunit using phosphorylation site-specific antibodies. J. Biol. Chem. 272 (1997) 5157-5166
    • (1997) J. Biol. Chem. , vol.272 , pp. 5157-5166
    • Tingley, W.G.1    Ehlers, M.D.2    Kameyama, K.3    Doherty, C.4    Ptak, J.B.5    Riley, C.T.6    Huganir, R.L.7
  • 34
    • 0037183734 scopus 로고    scopus 로고
    • Selective NR2B NMDA receptor antagonists are protective against staurosporine-induced apoptosis
    • Williams A.J., Dave J.R., Lu X.M., Ling G., and Tortella F.C. Selective NR2B NMDA receptor antagonists are protective against staurosporine-induced apoptosis. Eur. J. Pharmacol. 452 (2002) 135-136
    • (2002) Eur. J. Pharmacol. , vol.452 , pp. 135-136
    • Williams, A.J.1    Dave, J.R.2    Lu, X.M.3    Ling, G.4    Tortella, F.C.5
  • 35
    • 0034798601 scopus 로고    scopus 로고
    • Point mutations identify the glutamate binding pocket of the N-methyl-d-aspartate receptor as major site of Conantokin-G inhibition
    • Wittekindt B., Malany S., Schemm R., Otvos L., Maccecchini M.L., Laube B., and Betz H. Point mutations identify the glutamate binding pocket of the N-methyl-d-aspartate receptor as major site of Conantokin-G inhibition. Neuropharmacology 41 (2001) 753-761
    • (2001) Neuropharmacology , vol.41 , pp. 753-761
    • Wittekindt, B.1    Malany, S.2    Schemm, R.3    Otvos, L.4    Maccecchini, M.L.5    Laube, B.6    Betz, H.7
  • 36
    • 0028364252 scopus 로고
    • Transmembrane topology of two kainate receptor subunits revealed by N-glycosylation
    • Wo Z.G., and Oswald R.E. Transmembrane topology of two kainate receptor subunits revealed by N-glycosylation. Proc. Natl. Acad. Sci. U.S.A. 91 (1994) 7154-7158
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 7154-7158
    • Wo, Z.G.1    Oswald, R.E.2
  • 37
    • 0029071823 scopus 로고
    • Structural conservation of ion conduction pathways in K channels and glutamate receptors
    • Wood M.W., VanDongen H.M., and VanDongen A.M. Structural conservation of ion conduction pathways in K channels and glutamate receptors. Proc. Natl. Acad. Sci. U.S.A. 92 (1995) 4882-4886
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 4882-4886
    • Wood, M.W.1    VanDongen, H.M.2    VanDongen, A.M.3
  • 38
    • 0031023519 scopus 로고    scopus 로고
    • An alanine residue in the M3-M4 linker lines the glycine binding pocket of the N-methyl-d-aspartate receptor
    • Wood M.W., VanDongen H.M.A., and VanDongen A.M.J. An alanine residue in the M3-M4 linker lines the glycine binding pocket of the N-methyl-d-aspartate receptor. J. Biol. Chem. 272 (1997) 3532-3537
    • (1997) J. Biol. Chem. , vol.272 , pp. 3532-3537
    • Wood, M.W.1    VanDongen, H.M.A.2    VanDongen, A.M.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.