메뉴 건너뛰기




Volumn 290, Issue 2, 2015, Pages 797-804

Structural dynamics of the glycine-binding domain of the N-Methyl-D-aspartate receptor

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; ENERGY TRANSFER; FLUORESCENCE; LIGANDS; MOLECULES; PROTEINS; STRUCTURAL DYNAMICS;

EID: 84920915177     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.605436     Document Type: Article
Times cited : (37)

References (31)
  • 4
    • 72049124287 scopus 로고    scopus 로고
    • X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor
    • Sobolevsky, A. I., Rosconi, M. P., and Gouaux, E. (2009) X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor. Nature 462, 745-756
    • (2009) Nature , vol.462 , pp. 745-756
    • Sobolevsky, A.I.1    Rosconi, M.P.2    Gouaux, E.3
  • 5
    • 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
  • 6
    • 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
  • 7
    • 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. S., Jin, R., Liljefors, T., Mayer, M. L., Egebjerg, J., Larsen, I. K., 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
  • 8
    • 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
  • 9
    • 33745918325 scopus 로고    scopus 로고
    • Allosteric mechanism in AMPA receptors: A FRET-based investigation of conformational changes
    • Ramanoudjame, G., Du, M., Mankiewicz, K. A., and Jayaraman, V. (2006) Allosteric mechanism in AMPA receptors: a FRET-based investigation of conformational changes. Proc. Natl. Acad. Sci. U.S.A. 103, 10473-10478
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 10473-10478
    • Ramanoudjame, G.1    Du, M.2    Mankiewicz, K.A.3    Jayaraman, V.4
  • 10
    • 37849027018 scopus 로고    scopus 로고
    • Chemical interplay in the mechanism of partial agonist activation in α-ami-no-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors
    • Mankiewicz, K. A., Rambhadran, A., Wathen, L., and Jayaraman, V. (2008) Chemical interplay in the mechanism of partial agonist activation in α-ami-no-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors. Biochemistry 47, 398-404
    • (2008) Biochemistry , vol.47 , pp. 398-404
    • Mankiewicz, K.A.1    Rambhadran, A.2    Wathen, L.3    Jayaraman, V.4
  • 11
    • 0442279279 scopus 로고    scopus 로고
    • Structure and function of AMPA receptors
    • Gouaux, E. (2004) Structure and function of AMPA receptors. J. Physiol. 554, 249-253
    • (2004) J. Physiol. , vol.554 , pp. 249-253
    • Gouaux, E.1
  • 12
    • 42249101227 scopus 로고    scopus 로고
    • NMRspectroscopy of the ligandbinding core of ionotropic glutamate receptor 2 bound to 5-substituted willardiine partial agonists
    • Fenwick, M. K., and Oswald, R. E. (2008)NMRspectroscopy of the ligandbinding core of ionotropic glutamate receptor 2 bound to 5-substituted willardiine partial agonists. J. Mol. Biol. 378, 673-685
    • (2008) J. Mol. Biol. , vol.378 , pp. 673-685
    • Fenwick, M.K.1    Oswald, R.E.2
  • 13
    • 53249115359 scopus 로고    scopus 로고
    • Mechanism of partial agonism at the GluR2 AMPA receptor: Measurements of lobe orientation in solution
    • Maltsev, A. S., Ahmed, A. H., Fenwick, M. K., Jane, D. E., and Oswald, R. E. (2008) Mechanism of partial agonism at the GluR2 AMPA receptor: measurements of lobe orientation in solution. Biochemistry 47, 10600-10610
    • (2008) Biochemistry , vol.47 , pp. 10600-10610
    • Maltsev, A.S.1    Ahmed, A.H.2    Fenwick, M.K.3    Jane, D.E.4    Oswald, R.E.5
  • 14
    • 66149128065 scopus 로고    scopus 로고
    • Mechanisms of antagonism of the GluR2 AMPA receptor: Structure and dynamics of the complex of two willardiine antagonists with the glutamate binding domain
    • Ahmed, A. H., Thompson, M. D., Fenwick, M. K., Romero, B., Loh, A. P., Jane, D. E., Sondermann, H., and Oswald, R. E. (2009) Mechanisms of antagonism of the GluR2 AMPA receptor: structure and dynamics of the complex of two willardiine antagonists with the glutamate binding domain. Biochemistry 48, 3894-3903
    • (2009) Biochemistry , vol.48 , pp. 3894-3903
    • Ahmed, A.H.1    Thompson, M.D.2    Fenwick, M.K.3    Romero, B.4    Loh, A.P.5    Jane, D.E.6    Sondermann, H.7    Oswald, R.E.8
  • 15
    • 84884558766 scopus 로고    scopus 로고
    • Dynamics of cleft closure of the GluA2 ligand-binding domain in the presence of full and partial agonists revealed by hydro-gen-deuterium exchange
    • Ahmed, A. H., Ptak, C. P., Fenwick, M. K., Hsieh, C. L., Weiland, G. A., and Oswald, R. E. (2013) Dynamics of cleft closure of the GluA2 ligand-binding domain in the presence of full and partial agonists revealed by hydro-gen-deuterium exchange. J. Biol. Chem. 288, 27658-27666
    • (2013) J. Biol. Chem. , vol.288 , pp. 27658-27666
    • Ahmed, A.H.1    Ptak, C.P.2    Fenwick, M.K.3    Hsieh, C.L.4    Weiland, G.A.5    Oswald, R.E.6
  • 16
    • 79951847774 scopus 로고    scopus 로고
    • Structural landscape of isolated agonist-binding domains from single AMPA receptors
    • Landes, C. F., Rambhadran, A., Taylor, J. N., Salatan, F., and Jayaraman, V. (2011) Structural landscape of isolated agonist-binding domains from single AMPA receptors. Nat. Chem. Biol. 7, 168-173
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 168-173
    • Landes, C.F.1    Rambhadran, A.2    Taylor, J.N.3    Salatan, F.4    Jayaraman, V.5
  • 18
    • 84904199124 scopus 로고    scopus 로고
    • NMDAreceptor structures reveal subunit arrangement and pore architecture
    • Lee, C.-H., Lü, W., Michel, J. C., Goehring, A., Du, J., Song, X., and Gouaux, E. (2014)NMDAreceptor structures reveal subunit arrangement and pore architecture. Nature 511, 191-197
    • (2014) Nature , vol.511 , pp. 191-197
    • Lee, C.-H.1    Lü, W.2    Michel, J.C.3    Goehring, A.4    Du, J.5    Song, X.6    Gouaux, E.7
  • 19
    • 84901640125 scopus 로고    scopus 로고
    • Crystal structure of a heterotetrameric NMDA receptor ion channel
    • Karakas, E., and Furukawa, H. (2014) Crystal structure of a heterotetrameric NMDA receptor ion channel. Science 344, 992-997
    • (2014) Science , vol.344 , pp. 992-997
    • Karakas, E.1    Furukawa, H.2
  • 20
    • 79955750872 scopus 로고    scopus 로고
    • Conformational changes at the agonist binding domain of the N-methyl-D-aspartic acid receptor
    • Rambhadran, A., Gonzalez, J., and Jayaraman, V. (2011) Conformational changes at the agonist binding domain of the N-methyl-D-aspartic acid receptor. J. Biol. Chem. 286, 16953-16957
    • (2011) J. Biol. Chem. , vol.286 , pp. 16953-16957
    • Rambhadran, A.1    Gonzalez, J.2    Jayaraman, V.3
  • 21
    • 0038037859 scopus 로고    scopus 로고
    • Mechanisms of activation, inhibition and specificity: Crystal structures of the NMDA receptor NR1 ligandbinding core
    • Furukawa, H., and Gouaux, E. (2003) Mechanisms of activation, inhibition and specificity: crystal structures of the NMDA receptor NR1 ligandbinding core. EMBO J. 22, 2873-2885
    • (2003) EMBO J. , vol.22 , pp. 2873-2885
    • Furukawa, H.1    Gouaux, E.2
  • 22
    • 20444408992 scopus 로고    scopus 로고
    • Mechanism of partial agonist action at the NR1 subunit ofNMDAreceptors
    • Inanobe, A., Furukawa, H., and Gouaux, E. (2005) Mechanism of partial agonist action at the NR1 subunit ofNMDAreceptors. Neuron 47, 71-84
    • (2005) Neuron , vol.47 , pp. 71-84
    • Inanobe, A.1    Furukawa, H.2    Gouaux, E.3
  • 24
    • 84885433421 scopus 로고    scopus 로고
    • Conformational analysis of NMDA receptor GluN1, GluN2, and GluN3 ligand-binding domains reveals subtype-specific characteristics
    • Yao, Y., Belcher, J., Berger, A. J., Mayer, M. L., and Lau, A. Y. (2013) Conformational analysis of NMDA receptor GluN1, GluN2, and GluN3 ligand-binding domains reveals subtype-specific characteristics. Structure 21, 1788-1799
    • (2013) Structure , vol.21 , pp. 1788-1799
    • Yao, Y.1    Belcher, J.2    Berger, A.J.3    Mayer, M.L.4    Lau, A.Y.5
  • 25
    • 73149104141 scopus 로고    scopus 로고
    • An enhanced system for unnatural amino acid mutagenesis in E. Coli
    • Young, T. S., Ahmad, I., Yin, J. A., and Schultz, P. G. (2010) An enhanced system for unnatural amino acid mutagenesis in E. coli. J. Mol. Biol. 395, 361-374
    • (2010) J. Mol. Biol. , vol.395 , pp. 361-374
    • Young, T.S.1    Ahmad, I.2    Yin, J.A.3    Schultz, P.G.4
  • 26
    • 84879112632 scopus 로고    scopus 로고
    • Photobleaching lifetimes of cyanine fluorophores used for single-molecule Forster resonance energy transfer in the presence of various photoprotection systems
    • Cooper, D., Uhm, H., Tauzin, L. J., Poddar, N., and Landes, C. F. (2013) Photobleaching lifetimes of cyanine fluorophores used for single-molecule Forster resonance energy transfer in the presence of various photoprotection systems. Chembiochem 14, 1075-1080
    • (2013) Chembiochem , vol.14 , pp. 1075-1080
    • Cooper, D.1    Uhm, H.2    Tauzin, L.J.3    Poddar, N.4    Landes, C.F.5
  • 27
    • 57349131064 scopus 로고    scopus 로고
    • Human T-cell lymphotropic virus type 1 nucleocapsid protein-induced structural changes in transactivation response DNA hairpin measured by single-molecule fluorescence resonance energy transfer
    • Darugar, Q., Kim, H., Gorelick, R. J., and Landes, C. (2008) Human T-cell lymphotropic virus type 1 nucleocapsid protein-induced structural changes in transactivation response DNA hairpin measured by single-molecule fluorescence resonance energy transfer. J. Virol. 82, 12164-12171
    • (2008) J. Virol. , vol.82 , pp. 12164-12171
    • Darugar, Q.1    Kim, H.2    Gorelick, R.J.3    Landes, C.4
  • 29
    • 79951851154 scopus 로고    scopus 로고
    • Improved resolution of complex single-molecule FRET systems via wavelet shrinkage
    • Taylor, J. N., and Landes, C. F. (2011) Improved resolution of complex single-molecule FRET systems via wavelet shrinkage. J. Phys. Chem. B 115, 1105-1114
    • (2011) J. Phys. Chem. B , vol.115 , pp. 1105-1114
    • Taylor, J.N.1    Landes, C.F.2
  • 30
    • 74049099570 scopus 로고    scopus 로고
    • Denoising singlemolecule FRET trajectories with wavelets and Bayesian inference
    • Taylor, J. N., Makarov, D. E., and Landes, C. F. (2010) Denoising singlemolecule FRET trajectories with wavelets and Bayesian inference. Biophys. J. 98, 164-173
    • (2010) Biophys. J. , vol.98 , pp. 164-173
    • Taylor, J.N.1    Makarov, D.E.2    Landes, C.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.