메뉴 건너뛰기




Volumn 47, Issue 1, 2008, Pages 398-404

Chemical interplay in the mechanism of partial agonist activation in α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors

Author keywords

[No Author keywords available]

Indexed keywords

FLUORESCENCE; LIGANDS; MOLECULAR INTERACTIONS; NEUROLOGY; PROTEINS;

EID: 37849027018     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi702004b     Document Type: Article
Times cited : (13)

References (26)
  • 1
    • 16544383427 scopus 로고    scopus 로고
    • Ionotropic glutamate receptor recognition and activation
    • Oswald, R. E. (2004) Ionotropic glutamate receptor recognition and activation, Adv. Protein Chem. 68, 313-349.
    • (2004) Adv. Protein Chem , vol.68 , pp. 313-349
    • Oswald, R.E.1
  • 2
    • 1542373622 scopus 로고    scopus 로고
    • Emerging structural explanations of ionotropic glutamate receptor function
    • McFeeters, R. L., and Oswald, R. E. (2004) Emerging structural explanations of ionotropic glutamate receptor function, FASEB J. 18, 428-438.
    • (2004) FASEB J , vol.18 , pp. 428-438
    • McFeeters, R.L.1    Oswald, R.E.2
  • 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, Nat. Rev. Neurosci. 3, 91-101.
    • (2002) Nat. Rev. Neurosci , vol.3 , pp. 91-101
    • Madden, D.R.1
  • 4
    • 22944442256 scopus 로고    scopus 로고
    • The molecular pharmacology and cell biology of alpha-amino-3-hydroxy-5-methyl-4- isoxazolepropionic acid receptors
    • Palmer, C. L., Cotton, L., and Henley, J. M. (2005) The molecular pharmacology and cell biology of alpha-amino-3-hydroxy-5-methyl-4- isoxazolepropionic acid receptors, Pharmacol. Rev. 57, 253-277.
    • (2005) Pharmacol. Rev , vol.57 , pp. 253-277
    • Palmer, C.L.1    Cotton, L.2    Henley, J.M.3
  • 5
    • 33846828754 scopus 로고    scopus 로고
    • Role of the chemical interactions of the agonist in controlling α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor activation
    • Mankiewicz, K. A., Rambhadran, A., Du, M., Ramanoudjame, G., and Jayaraman, V. (2007) Role of the chemical interactions of the agonist in controlling α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor activation, Biochemistry 46, 1343-1349.
    • (2007) Biochemistry , vol.46 , pp. 1343-1349
    • Mankiewicz, K.A.1    Rambhadran, A.2    Du, M.3    Ramanoudjame, G.4    Jayaraman, V.5
  • 6
    • 2942718767 scopus 로고    scopus 로고
    • Chemistry and conformation of the ligand-binding domain of GluR2 subtype of glutamate receptors
    • Cheng, Q., and Jayaraman, V. (2004) Chemistry and conformation of the ligand-binding domain of GluR2 subtype of glutamate receptors, J. Biol. Chem. 279, 26346-26350.
    • (2004) J. Biol. Chem , vol.279 , pp. 26346-26350
    • Cheng, Q.1    Jayaraman, V.2
  • 7
    • 33644846012 scopus 로고    scopus 로고
    • Evolution of glutamate interactions during binding to a glutamate receptor
    • Cheng, Q., Du, M., Ramanoudjame, G., and Jayaraman, V. (2005) Evolution of glutamate interactions during binding to a glutamate receptor, Nat. Chem. Biol. 1, 329-332.
    • (2005) Nat. Chem. Biol , vol.1 , pp. 329-332
    • Cheng, Q.1    Du, M.2    Ramanoudjame, G.3    Jayaraman, V.4
  • 8
    • 37349129888 scopus 로고    scopus 로고
    • Glutamate receptors as seen by light: Spectroscopic studies of structure-function relationships
    • Mankiewicz, K. A., and Jayaraman, V. (2007) Glutamate receptors as seen by light: Spectroscopic studies of structure-function relationships, Braz. J. Med. Biol. Res. 40, 1419-1427.
    • (2007) Braz. J. Med. Biol. Res , vol.40 , pp. 1419-1427
    • Mankiewicz, K.A.1    Jayaraman, V.2
  • 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
    • 0028357664 scopus 로고
    • Willardiines differentiate agonist binding sites for kainate- versus AMPA-preferring glutamate receptors in DRG and hippocampal neurons
    • Wong, L. A., Mayer, M. L., Jane, D. E., and Watkins, J. C. (1994) Willardiines differentiate agonist binding sites for kainate- versus AMPA-preferring glutamate receptors in DRG and hippocampal neurons, J. Neurosci. 14, 3881-3897.
    • (1994) J. Neurosci , vol.14 , pp. 3881-3897
    • Wong, L.A.1    Mayer, M.L.2    Jane, D.E.3    Watkins, J.C.4
  • 11
    • 0026556811 scopus 로고
    • Activation and desensitization of AMPA/kainate receptors by novel derivatives of willardiine
    • Patneau, D. K., Mayer, M. L., Jane, D. E., and Watkins, J. C. (1992) Activation and desensitization of AMPA/kainate receptors by novel derivatives of willardiine, J. Neurosci. 12, 595-606.
    • (1992) J. Neurosci , vol.12 , pp. 595-606
    • Patneau, D.K.1    Mayer, M.L.2    Jane, D.E.3    Watkins, J.C.4
  • 12
    • 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
  • 13
    • 0038219813 scopus 로고    scopus 로고
    • Probing the function, conformational plasticity, and dimer-dimer contacts of the GluR2 ligand-binding core: Studies of 5-substituted willardiines and GluR2 S1S2 in the crystal
    • Jin, R., and Gouaux, E. (2003) Probing the function, conformational plasticity, and dimer-dimer contacts of the GluR2 ligand-binding core: Studies of 5-substituted willardiines and GluR2 S1S2 in the crystal, Biochemistry 42, 5201-5213.
    • (2003) Biochemistry , vol.42 , pp. 5201-5213
    • Jin, R.1    Gouaux, E.2
  • 14
    • 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. A., 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.A.1    Gouaux, E.2
  • 15
    • 0038625032 scopus 로고    scopus 로고
    • Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic adjustment of agonist-induced conformational changes
    • Armstrong, N., Mayer, M., and Gouaux, E. (2003) Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic adjustment of agonist-induced conformational changes, Proc. Natl. Acad. Sci. U.S.A. 100, 5736-5741.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 5736-5741
    • Armstrong, N.1    Mayer, M.2    Gouaux, E.3
  • 16
    • 33749059766 scopus 로고    scopus 로고
    • Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor
    • Armstrong, N., Jasti, J., Beich-Frandsen, M., and 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
  • 17
    • 0038037859 scopus 로고    scopus 로고
    • Mechanisms of activation, inhibition and specificity: Crystal stmctures of the NMDA receptor NR1 ligand-binding core
    • Furukawa, H., and Gouaux, E. (2003) Mechanisms of activation, inhibition and specificity: Crystal stmctures of the NMDA receptor NR1 ligand-binding core, EMBO J. 22, 2873-2885.
    • (2003) EMBO J , vol.22 , pp. 2873-2885
    • Furukawa, H.1    Gouaux, E.2
  • 18
    • 15744405987 scopus 로고    scopus 로고
    • Conformational changes in the ligand-binding domain of a functional ionotropic glutamate receptor
    • Du, M., Reid, S. A., and Jayaraman, V. (2005) Conformational changes in the ligand-binding domain of a functional ionotropic glutamate receptor, J. Biol. Chem. 280, 8633-6.
    • (2005) J. Biol. Chem , vol.280 , pp. 8633-8636
    • Du, M.1    Reid, S.A.2    Jayaraman, V.3
  • 19
    • 0039592758 scopus 로고    scopus 로고
    • Ligand - protein interactions in the glutamate receptor
    • Jayaraman, V., Keesey, R., and Madden, D. R. (2000) Ligand - protein interactions in the glutamate receptor, Biochemistry 39, 8693-8697.
    • (2000) Biochemistry , vol.39 , pp. 8693-8697
    • Jayaraman, V.1    Keesey, R.2    Madden, D.R.3
  • 20
    • 1542319994 scopus 로고    scopus 로고
    • Spectroscopic and kinetic methods for ligand-protein interactions of glutamate receptor
    • Jayaraman, V. (2004) Spectroscopic and kinetic methods for ligand-protein interactions of glutamate receptor. Methods Enzymol. 380, 170-187.
    • (2004) Methods Enzymol , vol.380 , pp. 170-187
    • Jayaraman, V.1
  • 21
    • 0031471216 scopus 로고    scopus 로고
    • Overexpression of a glutamate receptor (GluR2) ligand binding domain in Escherichia coli: Application of a novel protein folding screen
    • Chen, G.-Q., and Gouaux, E. (1997) Overexpression of a glutamate receptor (GluR2) ligand binding domain in Escherichia coli: Application of a novel protein folding screen, Proc. Natl. Acad. Sci. U.S.A. 94, 13431-13436.
    • (1997) Proc. Natl. Acad. Sci. U.S.A , vol.94 , pp. 13431-13436
    • Chen, G.-Q.1    Gouaux, E.2
  • 22
    • 0037022201 scopus 로고    scopus 로고
    • A vibrational spectroscopic investigation of interactions of agonists with GluR0, a prokaryotic glutamate receptor
    • Cheng, Q., Thiran, S., Yernool, D., Gouaux, E., and Jayaraman, V. (2002) A vibrational spectroscopic investigation of interactions of agonists with GluR0, a prokaryotic glutamate receptor, Biochemistry 41, 1602-1608.
    • (2002) Biochemistry , vol.41 , pp. 1602-1608
    • Cheng, Q.1    Thiran, S.2    Yernool, D.3    Gouaux, E.4    Jayaraman, V.5
  • 23
    • 0024422960 scopus 로고
    • Investigation of membrane-protein structure using Fourier-transform infrared-spectroscopy
    • Chapman, D., Jackson, M., and Haris, P. I. (1989) Investigation of membrane-protein structure using Fourier-transform infrared-spectroscopy, Biochem. Soc. Trans. 17, 617-619.
    • (1989) Biochem. Soc. Trans , vol.17 , pp. 617-619
    • Chapman, D.1    Jackson, M.2    Haris, P.I.3
  • 24
    • 34250318954 scopus 로고    scopus 로고
    • Dynamics of the S1S2 glutamate binding domain of GluR2 measured using 19F NMR spectroscopy
    • Ahmed, A. H., Loh, A. P., Jane, D. E., and Oswald, R. E. (2007) Dynamics of the S1S2 glutamate binding domain of GluR2 measured using 19F NMR spectroscopy, J. Biol. Chem. 282, 12773-12784.
    • (2007) J. Biol. Chem , vol.282 , pp. 12773-12784
    • Ahmed, A.H.1    Loh, A.P.2    Jane, D.E.3    Oswald, R.E.4
  • 25
    • 0037143575 scopus 로고    scopus 로고
    • Structural mobility of the extracellular ligand-binding core of an ionotropic glutamate receptor. Analysis of NMR relaxation dynamics
    • McFeeters, R. L., and Oswald, R. E. (2002) Structural mobility of the extracellular ligand-binding core of an ionotropic glutamate receptor. Analysis of NMR relaxation dynamics, Biochemistry 41, 10472-10481.
    • (2002) Biochemistry , vol.41 , pp. 10472-10481
    • McFeeters, R.L.1    Oswald, R.E.2
  • 26
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • Koshland, D. E., Jr., Nemethy, G., and Filmer, D. (1966) Comparison of experimental binding data and theoretical models in proteins containing subunits, Biochemistry 5, 365-385.
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • Koshland Jr., D.E.1    Nemethy, G.2    Filmer, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.