메뉴 건너뛰기




Volumn 106, Issue 30, 2009, Pages 12329-12334

Energetics of glutamate receptor ligand binding domain dimer assembly are modulated by allosteric ions

Author keywords

Allosteric modulation; Analytical ultracentrifugation; Desensitization; Ion channels; Thermodynamics

Indexed keywords

CALCIUM ION; CHLORIDE ION; DIMER; GLUTAMATE RECEPTOR; GLUTAMATE RECEPTOR 6; GLUTAMATE RECEPTOR DELTA2; ION CHANNEL; KAINIC ACID RECEPTOR; MUTANT PROTEIN; SODIUM ION; UNCLASSIFIED DRUG;

EID: 68149092677     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0904175106     Document Type: Article
Times cited : (41)

References (31)
  • 1
    • 0032215090 scopus 로고    scopus 로고
    • Allosteric receptors after 30 years
    • Changeux JP, Edelstein SJ (1998) Allosteric receptors after 30 years. Neuron 21:959-980.
    • (1998) Neuron , vol.21 , pp. 959-980
    • Changeux, J.P.1    Edelstein, S.J.2
  • 2
    • 0037118049 scopus 로고    scopus 로고
    • Mechanism of glutamate receptor desensitization
    • Sun Y, et al. (2002) Mechanism of glutamate receptor desensitization. Nature 417:245-253.
    • (2002) Nature , vol.417 , pp. 245-253
    • Sun, Y.1
  • 3
    • 25644454403 scopus 로고    scopus 로고
    • Mechanism of positive allosteric modulators acting on AMPA receptors
    • Jin R, et al. (2005) Mechanism of positive allosteric modulators acting on AMPA receptors. J Neurosci 25:9027-9036.
    • (2005) J Neurosci , vol.25 , pp. 9027-9036
    • Jin, R.1
  • 4
    • 34147179943 scopus 로고    scopus 로고
    • Ivermectin interaction with transmembrane helices reveals widespread rearrangements during opening of P2X receptor channels
    • Silberberg SD, Li M, Swartz KJ (2007) Ivermectin interaction with transmembrane helices reveals widespread rearrangements during opening of P2X receptor channels. Neuron 54:263-274.
    • (2007) Neuron , vol.54 , pp. 263-274
    • Silberberg, S.D.1    Li, M.2    Swartz, K.J.3
  • 5
    • 0025050847 scopus 로고
    • Structural and functional characterization of the gamma 1 subunit of GABAA/benzodiazepine receptors
    • Ymer S, et al. (1990) Structural and functional characterization of the gamma 1 subunit of GABAA/benzodiazepine receptors. EMBO J 9:3261-3267.
    • (1990) EMBO J , vol.9 , pp. 3261-3267
    • Ymer, S.1
  • 6
    • 0037088834 scopus 로고    scopus 로고
    • External anions and cations distinguish between AMPA and kainate receptor gating mechanisms
    • Bowie D (2002) External anions and cations distinguish between AMPA and kainate receptor gating mechanisms. J Physiol 539:725-733.
    • (2002) J Physiol , vol.539 , pp. 725-733
    • Bowie, D.1
  • 7
    • 0042199046 scopus 로고    scopus 로고
    • A role for extracellular Na+ in the channel gating of native and recombinant kainate receptors
    • Paternain AV, Cohen A, Stern-Bach Y, Lerma J (2003) A role for extracellular Na+ in the channel gating of native and recombinant kainate receptors. J Neurosci 23:8641-8648.
    • (2003) J Neurosci , vol.23 , pp. 8641-8648
    • Paternain, A.V.1    Cohen, A.2    Stern-Bach, Y.3    Lerma, J.4
  • 8
    • 33847769253 scopus 로고    scopus 로고
    • Structure and mechanism of kainate receptor modulation by anions
    • Plested AJ, Mayer ML (2007) Structure and mechanism of kainate receptor modulation by anions. Neuron 53:829-841.
    • (2007) Neuron , vol.53 , pp. 829-841
    • Plested, A.J.1    Mayer, M.L.2
  • 9
    • 44649169115 scopus 로고    scopus 로고
    • Molecular basis of kainate receptor modulation by sodium
    • Plested AJ, Vijayan R, Biggin PC, Mayer ML (2008) Molecular basis of kainate receptor modulation by sodium. Neuron 58:720-735.
    • (2008) Neuron , vol.58 , pp. 720-735
    • Plested, A.J.1    Vijayan, R.2    Biggin, P.C.3    Mayer, M.L.4
  • 10
    • 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, 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
  • 11
    • 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 ML, Olson R, 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
  • 12
    • 13444281913 scopus 로고    scopus 로고
    • Structure of the kainate receptor subunit GluR6 agonist-binding domain complexed with domoic acid
    • Nanao MH, Green T, Stern-Bach Y, Heinemann SF, Choe S (2005) Structure of the kainate receptor subunit GluR6 agonist-binding domain complexed with domoic acid. Proc Natl Acad Sci USA 102:1708-1713.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 1708-1713
    • Nanao, M.H.1    Green, T.2    Stern-Bach, Y.3    Heinemann, S.F.4    Choe, S.5
  • 13
    • 33749059766 scopus 로고    scopus 로고
    • Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor
    • Armstrong N, Jasti J, Beich-Frandsen M, Gouaux E (2006) Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor. Cell 127:85-97.
    • (2006) Cell , vol.127 , pp. 85-97
    • Armstrong, N.1    Jasti, J.2    Beich-Frandsen, M.3    Gouaux, E.4
  • 15
    • 67349279392 scopus 로고    scopus 로고
    • Stability of ligand-binding domain dimer assembly controls kainate receptor desensitization
    • Chaudhry C, Weston MC, Schuck P, Rosenmund C, Mayer ML (2009) Stability of ligand-binding domain dimer assembly controls kainate receptor desensitization. EMBO J 28:1518-1530.
    • (2009) EMBO J , vol.28 , pp. 1518-1530
    • Chaudhry, C.1    Weston, M.C.2    Schuck, P.3    Rosenmund, C.4    Mayer, M.L.5
  • 16
    • 35348840286 scopus 로고    scopus 로고
    • Ionotropic glutamate-like receptor delta2 binds D-serine and glycine
    • Naur P, et al. (2007) Ionotropic glutamate-like receptor delta2 binds D-serine and glycine. Proc Natl Acad Sci USA 104:14116-14121.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 14116-14121
    • Naur, P.1
  • 17
    • 65549085773 scopus 로고    scopus 로고
    • Selectivity and cooperativity of modulatory ions in a neurotransmitter receptor
    • Vijayan R, Plested AJ, Mayer ML, Biggin PC (2009) Selectivity and cooperativity of modulatory ions in a neurotransmitter receptor. Biophys J 96:1751-1760.
    • (2009) Biophys J , vol.96 , pp. 1751-1760
    • Vijayan, R.1    Plested, A.J.2    Mayer, M.L.3    Biggin, P.C.4
  • 18
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • Schuck P (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophys J 78:1606-1619.
    • (2000) Biophys J , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 19
    • 1442274756 scopus 로고    scopus 로고
    • Sedimentation equilibrium analysis of protein interactions with global implicit mass conservation constraints and systematic noise decomposition
    • Vistica J, et al. (2004) Sedimentation equilibrium analysis of protein interactions with global implicit mass conservation constraints and systematic noise decomposition. Anal Biochem 326:234-256.
    • (2004) Anal Biochem , vol.326 , pp. 234-256
    • Vistica, J.1
  • 20
    • 27744500994 scopus 로고    scopus 로고
    • Subunit arrangement and function in NMDA receptors
    • Furukawa H, Singh SK, Mancusso R, Gouaux E (2005) Subunit arrangement and function in NMDA receptors. Nature 438:185-192.
    • (2005) Nature , vol.438 , pp. 185-192
    • Furukawa, H.1    Singh, S.K.2    Mancusso, R.3    Gouaux, E.4
  • 21
    • 49149095000 scopus 로고    scopus 로고
    • Molecular mechanism of ligand recognition by NR3 subtype glutamate receptors
    • Yao Y, Harrison CB, Freddolino PL, Schulten K, Mayer ML (2008) Molecular mechanism of ligand recognition by NR3 subtype glutamate receptors. EMBO J 27:2158-2170.
    • (2008) EMBO J , vol.27 , pp. 2158-2170
    • Yao, Y.1    Harrison, C.B.2    Freddolino, P.L.3    Schulten, K.4    Mayer, M.L.5
  • 22
    • 0034663022 scopus 로고    scopus 로고
    • The Lurcher mutation identifies delta 2 as an AMPA/kainate receptor-like channel that is potentiated by Ca(2+)
    • Wollmuth LP, et al. (2000) The Lurcher mutation identifies delta 2 as an AMPA/kainate receptor-like channel that is potentiated by Ca(2+). J Neurosci 20:5973-5980.
    • (2000) J Neurosci , vol.20 , pp. 5973-5980
    • Wollmuth, L.P.1
  • 23
    • 59649125327 scopus 로고    scopus 로고
    • Modulation of the dimer interface at ionotropic glutamate-like receptor delta2 by D-serine and extracellular calcium
    • Hansen KB, et al. (2009) Modulation of the dimer interface at ionotropic glutamate-like receptor delta2 by D-serine and extracellular calcium. J Neurosci 29:907-917.
    • (2009) J Neurosci , vol.29 , pp. 907-917
    • Hansen, K.B.1
  • 24
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • Garcia De La Torre J, Huertas ML, Carrasco B (2000) Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys J 78:719-730.
    • (2000) Biophys J , vol.78 , pp. 719-730
    • Garcia De La Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 25
    • 0018199151 scopus 로고
    • Life time and elementary conductance of the channels mediating the excitatory effects of acetylcholine in Aplysia neurones
    • Ascher P, Marty A, Neild TO (1978) Life time and elementary conductance of the channels mediating the excitatory effects of acetylcholine in Aplysia neurones. J Physiol 278:177-206.
    • (1978) J Physiol , vol.278 , pp. 177-206
    • Ascher, P.1    Marty, A.2    Neild, T.O.3
  • 26
    • 0030031856 scopus 로고    scopus 로고
    • Use-dependent blockers and exit rate of the last ion from the multi-ion pore of a K+-channel
    • Baukrowitz T, Yellen G (1996) Use-dependent blockers and exit rate of the last ion from the multi-ion pore of a K+-channel. Science 271:653-656.
    • (1996) Science , vol.271 , pp. 653-656
    • Baukrowitz, T.1    Yellen, G.2
  • 27
    • 0035499892 scopus 로고    scopus 로고
    • Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution
    • Zhou Y, Morais-Cabral JH, Kaufman A, MacKinnon R (2001) Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution. Nature 414:43-48.
    • (2001) Nature , vol.414 , pp. 43-48
    • Zhou, Y.1    Morais-Cabral, J.H.2    Kaufman, A.3    MacKinnon, R.4
  • 28
    • 58049192996 scopus 로고    scopus 로고
    • Engineering a high-affinity allosteric binding site for divalent cations in kainate receptors
    • Plested AJ, Mayer ML (2009) Engineering a high-affinity allosteric binding site for divalent cations in kainate receptors. Neuropharmacology 56:114-120.
    • (2009) Neuropharmacology , vol.56 , pp. 114-120
    • Plested, A.J.1    Mayer, M.L.2
  • 30
    • 1242293631 scopus 로고    scopus 로고
    • Regulation of AMPA receptor gating by ligand binding core dimers
    • Horning MS, Mayer ML (2004) Regulation of AMPA receptor gating by ligand binding core dimers. Neuron 41:379-388.
    • (2004) Neuron , vol.41 , pp. 379-388
    • Horning, M.S.1    Mayer, M.L.2
  • 31
    • 13844266202 scopus 로고    scopus 로고
    • Crystal structures of the GluR5 and GluR6 ligand binding cores: Molecular mechanisms underlying kainate receptor selectivity
    • Mayer ML (2005) Crystal structures of the GluR5 and GluR6 ligand binding cores: Molecular mechanisms underlying kainate receptor selectivity. Neuron 45:539-552.
    • (2005) Neuron , vol.45 , pp. 539-552
    • Mayer, M.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.