메뉴 건너뛰기




Volumn 27, Issue 7, 2009, Pages 813-821

Molecular modeling of ligand-receptor interactions in GABAC receptor

Author keywords

GABA; GABAC receptor; Ligand receptor interactions; Molecular dynamics; TPMPA

Indexed keywords

BINDING FORCES; BINDING ORIENTATIONS; GABA; GABAC RECEPTOR; HOMOLOGY MODELS; LIGAND-RECEPTOR INTERACTIONS; MOLECULAR DYNAMICS SIMULATIONS; SALT BRIDGES; TPMPA;

EID: 61449136689     PISSN: 10933263     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmgm.2008.12.004     Document Type: Article
Times cited : (24)

References (39)
  • 1
    • 0034692175 scopus 로고    scopus 로고
    • GABA-activated ligand gated ion channels: medicinal chemistry and molecular biology
    • Chebib M., and Johnston G.A.R. GABA-activated ligand gated ion channels: medicinal chemistry and molecular biology. J. Med. Chem. 43 (2000) 1427-1447
    • (2000) J. Med. Chem. , vol.43 , pp. 1427-1447
    • Chebib, M.1    Johnston, G.A.R.2
  • 3
    • 0032587999 scopus 로고    scopus 로고
    • C receptor ρ subunits are heterogeneously expressed in the human CNS and form homo- and heterooligomers with distinct physical properties
    • C receptor ρ subunits are heterogeneously expressed in the human CNS and form homo- and heterooligomers with distinct physical properties. Eur. J. Neurosci. 11 (1999) 41-50
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 41-50
    • Enz, R.1    Cutting, G.R.2
  • 4
    • 0034745280 scopus 로고    scopus 로고
    • Study of a GABAC receptor antagonist on sleep-waking behavior in rats
    • Arnaud C., Gauthier P., and Gottesmann C. Study of a GABAC receptor antagonist on sleep-waking behavior in rats. Psychopharmacology 154 (2001) 415-419
    • (2001) Psychopharmacology , vol.154 , pp. 415-419
    • Arnaud, C.1    Gauthier, P.2    Gottesmann, C.3
  • 5
    • 0035902009 scopus 로고    scopus 로고
    • Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors
    • Brejc K., van Dijk W.J., Klaassen R.V., Schuurmans M., van der Oost J., Smit A.B., and Sixma T.K. Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors. Nature 411 (2001) 269-276
    • (2001) Nature , vol.411 , pp. 269-276
    • Brejc, K.1    van Dijk, W.J.2    Klaassen, R.V.3    Schuurmans, M.4    van der Oost, J.5    Smit, A.B.6    Sixma, T.K.7
  • 6
    • 1842475289 scopus 로고    scopus 로고
    • Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures
    • Celie P.H.N., van Rossum-Fikkert S.E., van Dijk W.J., Brejc K., Smit A.B., and Sixma T.K. Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures. Neuron 41 (2004) 907-914
    • (2004) Neuron , vol.41 , pp. 907-914
    • Celie, P.H.N.1    van Rossum-Fikkert, S.E.2    van Dijk, W.J.3    Brejc, K.4    Smit, A.B.5    Sixma, T.K.6
  • 7
    • 27144473613 scopus 로고    scopus 로고
    • Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations
    • Hansen S.B., Sulzenbacher G., Huxford T., Marchot P., Taylor P., and Bourne Y. Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations. EMBO J. 24 (2005) 3635-3646
    • (2005) EMBO J. , vol.24 , pp. 3635-3646
    • Hansen, S.B.1    Sulzenbacher, G.2    Huxford, T.3    Marchot, P.4    Taylor, P.5    Bourne, Y.6
  • 8
    • 14844323974 scopus 로고    scopus 로고
    • A chimera encoding the fusion of an acetylcholine-binding protein to an ion channel is stabilized in a state close to the desensitized form of ligand-gated ion channels
    • Grutter T., Prado de Carvalho L., Dufresne V., Taly A., Fischer M., and Changeux J.-P. A chimera encoding the fusion of an acetylcholine-binding protein to an ion channel is stabilized in a state close to the desensitized form of ligand-gated ion channels. C. R. Biol. 328 (2005) 223-234
    • (2005) C. R. Biol. , vol.328 , pp. 223-234
    • Grutter, T.1    Prado de Carvalho, L.2    Dufresne, V.3    Taly, A.4    Fischer, M.5    Changeux, J.-P.6
  • 10
    • 33644774783 scopus 로고    scopus 로고
    • Molecular modeling of the GABAC receptor ligand-binding domain
    • Harrison N.J., and Lummis S.C.R. Molecular modeling of the GABAC receptor ligand-binding domain. J. Mol. Model. 12 (2005) 317-324
    • (2005) J. Mol. Model. , vol.12 , pp. 317-324
    • Harrison, N.J.1    Lummis, S.C.R.2
  • 15
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4 Å resolution
    • Unwin N. Refined structure of the nicotinic acetylcholine receptor at 4 Å resolution. J. Mol. Biol. 346 (2005) 967-989
    • (2005) J. Mol. Biol. , vol.346 , pp. 967-989
    • Unwin, N.1
  • 16
    • 0036304564 scopus 로고    scopus 로고
    • Activation of the nicotinic acetylcholine receptor involves a switch in conformation of the α subunits
    • Unwin N., Miyazawa A., Li J., and Fujiyoshi Y. Activation of the nicotinic acetylcholine receptor involves a switch in conformation of the α subunits. J. Mol. Biol. 319 (2002) 1165-1176
    • (2002) J. Mol. Biol. , vol.319 , pp. 1165-1176
    • Unwin, N.1    Miyazawa, A.2    Li, J.3    Fujiyoshi, Y.4
  • 21
    • 33846041078 scopus 로고    scopus 로고
    • The Universal Protein Resource (UniProt)
    • UniProt Consortium. The Universal Protein Resource (UniProt). Nucleic Acids Res. 35 Database issue (2007) D193-D197
    • (2007) Nucleic Acids Res. , vol.35 , Issue.Database issue
    • UniProt Consortium1
  • 22
    • 0035967880 scopus 로고    scopus 로고
    • FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • Shi J., Blundell T.L., and Mizuguchi K. FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J. Mol. Biol. 310 (2001) 243-257
    • (2001) J. Mol. Biol. , vol.310 , pp. 243-257
    • Shi, J.1    Blundell, T.L.2    Mizuguchi, K.3
  • 23
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Šali A., and Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234 (1993) 779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Šali, A.1    Blundell, T.L.2
  • 24
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26 (1993) 283-291
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 28
    • 0036890178 scopus 로고    scopus 로고
    • Fast, efficient generation of high-quality atomic charges. AM1-BCC model: II. Parameterization and validation
    • Jakalian A., Jack D.B., and Bayly C.I. Fast, efficient generation of high-quality atomic charges. AM1-BCC model: II. Parameterization and validation. J. Comput. Chem. 23 (2002) 1623-1641
    • (2002) J. Comput. Chem. , vol.23 , pp. 1623-1641
    • Jakalian, A.1    Jack, D.B.2    Bayly, C.I.3
  • 30
    • 0036288851 scopus 로고    scopus 로고
    • Characterization and prediction of linker sequences of multi-domain proteins by a neural network
    • Miyazaki S., Kuroda Y., and Yokoyama S. Characterization and prediction of linker sequences of multi-domain proteins by a neural network. J. Struct. Funct. Genom. 15 (2002) 37-51
    • (2002) J. Struct. Funct. Genom. , vol.15 , pp. 37-51
    • Miyazaki, S.1    Kuroda, Y.2    Yokoyama, S.3
  • 31
    • 0343851085 scopus 로고    scopus 로고
    • Functional and pharmacological properties of GABAρ1Δ51 receptors
    • Demuro A., Martínez-Torres A., and Miledi R. Functional and pharmacological properties of GABAρ1Δ51 receptors. Neurosci. Res. 36 (2000) 141-146
    • (2000) Neurosci. Res. , vol.36 , pp. 141-146
    • Demuro, A.1    Martínez-Torres, A.2    Miledi, R.3
  • 32
    • 0028171915 scopus 로고
    • 1 GABA channels: activation properties and domains
    • 1 GABA channels: activation properties and domains. Recept. Channels 2 (1994) 227-236
    • (1994) Recept. Channels , vol.2 , pp. 227-236
    • Amin, J.1    Weiss, D.S.2
  • 33
    • 1642377868 scopus 로고    scopus 로고
    • Modelling extracellular domains of GABA-A receptors: subtypes 1, 2, 3 and 5
    • Chou K.C. Modelling extracellular domains of GABA-A receptors: subtypes 1, 2, 3 and 5. Biochem. Biophys. Res. Commun. 316 (2004) 636-642
    • (2004) Biochem. Biophys. Res. Commun. , vol.316 , pp. 636-642
    • Chou, K.C.1
  • 36
    • 10644270878 scopus 로고    scopus 로고
    • 2 subunit produces a spontaneously open channel: a trigger for channel activation
    • 2 subunit produces a spontaneously open channel: a trigger for channel activation. J. Neurosci. 24 (2004) 11226-11235
    • (2004) J. Neurosci. , vol.24 , pp. 11226-11235
    • Newell, J.G.1    McDevitt, R.A.2    Czajkowski, C.3
  • 37
    • 4444351490 scopus 로고    scopus 로고
    • Empirical force fields for biological macromolecules: overview and issues
    • Mackerell Jr. A.D. Empirical force fields for biological macromolecules: overview and issues. J. Comput. Chem. 25 (2004) 1584-1604
    • (2004) J. Comput. Chem. , vol.25 , pp. 1584-1604
    • Mackerell Jr., A.D.1
  • 38
    • 0034624393 scopus 로고    scopus 로고
    • A computational study of cation-π Interactions vs salt bridges in aqueous media: implications for protein engineering
    • Gallivan J.P., and Dougherty D.A. A computational study of cation-π Interactions vs salt bridges in aqueous media: implications for protein engineering. J. Am. Chem. Soc. 122 (2000) 870-874
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 870-874
    • Gallivan, J.P.1    Dougherty, D.A.2
  • 39
    • 0028883463 scopus 로고
    • A single histidine residue is essential for zinc inhibition of GABA ρ1 receptors
    • Wang T.-L., Hackam A., Guggino W.B., and Cutting G.R. A single histidine residue is essential for zinc inhibition of GABA ρ1 receptors. J. Neurosci. 15 (1995) 7684-7691
    • (1995) J. Neurosci. , vol.15 , pp. 7684-7691
    • Wang, T.-L.1    Hackam, A.2    Guggino, W.B.3    Cutting, G.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.