메뉴 건너뛰기




Volumn 21, Issue 12, 2004, Pages 2270-2278

Studies of binding modes of (S)-mephenytoin to wild types and mutants of cytochrome P450 2C19 and 2C9 using homology modeling and computational docking

Author keywords

Binding mode; Computational docking; Cytochrome P450 2C19; Homology modeling

Indexed keywords

CYTOCHROME P450 2C19; CYTOCHROME P450 2C9; MEPHENYTOIN;

EID: 17644378105     PISSN: 07248741     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11095-004-7680-8     Document Type: Article
Times cited : (25)

References (39)
  • 1
    • 0025763625 scopus 로고
    • Cloning and expression of complementary DNAs for multiple members of the human cytochrome P450IIC subfamily
    • M. Romkes, M. B. Faletto, J. A. Blaisdell, J. L. Raucy, and J. A. Goldstein. Cloning and expression of complementary DNAs for multiple members of the human cytochrome P450IIC subfamily. Biochemistry 30:3247-3255 (1991).
    • (1991) Biochemistry , vol.30 , pp. 3247-3255
    • Romkes, M.1    Faletto, M.B.2    Blaisdell, J.A.3    Raucy, J.L.4    Goldstein, J.A.5
  • 2
    • 0027445449 scopus 로고
    • Isolation and characterization of human liver cytochrome P450 2C19: Correlation between 2C19 and S-mephenytoin 4′-hydroxylation
    • S. A. Wrighton, J. C. Stevens, G. W. Becker, and M. Vanden-Branden. Isolation and characterization of human liver cytochrome P450 2C19: correlation between 2C19 and S-mephenytoin 4′-hydroxylation. Arch. Biochem. Biophys. 306:240-245 (1993).
    • (1993) Arch. Biochem. Biophys. , vol.306 , pp. 240-245
    • Wrighton, S.A.1    Stevens, J.C.2    Becker, G.W.3    Vanden-Branden, M.4
  • 6
    • 0028044085 scopus 로고
    • Identification of a new genetic defect responsible for the polymorphism of S-mephenytoin metabolism in Japanese
    • S. M. F. de Morais, G. R. Wilkinson, J. Blaisdell, K. Nakamura, U. A. Meyer, and J. A. Goldstein. Identification of a new genetic defect responsible for the polymorphism of S-mephenytoin metabolism in Japanese. Mol. Pharmacol. 46:594-598 (1994).
    • (1994) Mol. Pharmacol. , vol.46 , pp. 594-598
    • De Morais, S.M.F.1    Wilkinson, G.R.2    Blaisdell, J.3    Nakamura, K.4    Meyer, U.A.5    Goldstein, J.A.6
  • 7
    • 8244249473 scopus 로고    scopus 로고
    • Differences in the incidence of the CYP2C19 polymorphism affecting the S-mephenytoin phenotype in Chinese Han and Bai populations and identification of a new rare CYP2C19 mutant allele
    • Z. S. Xiao, J. A. Goldstein, H.-G. Xie, J. Blaisdell, W. Wang, C.-H. Jiang, F.-X. Yan, N. He, S.-L. Huang, Z.-H. Xu, and H.-H. Zhou. Differences in the incidence of the CYP2C19 polymorphism affecting the S-mephenytoin phenotype in Chinese Han and Bai populations and identification of a new rare CYP2C19 mutant allele. J. Pharmacol. Exp. Ther. 281:604-609 (1997).
    • (1997) J. Pharmacol. Exp. Ther. , vol.281 , pp. 604-609
    • Xiao, Z.S.1    Goldstein, J.A.2    Xie, H.-G.3    Blaisdell, J.4    Wang, W.5    Jiang, C.-H.6    Yan, F.-X.7    He, N.8    Huang, S.-L.9    Xu, Z.-H.10    Zhou, H.-H.11
  • 11
    • 0032797302 scopus 로고    scopus 로고
    • A novel transversion in the intron 5 donor splice junction of CYP2C19 and a sequence polymorphism in exon 3 contribute to the poor metabolizer phenotype for the anticonvulsant drug S-mephenytoin
    • G. C. Ibeanu, J. Blaisdell, R. J. Gerguson, B. I. Ghanayem, K. Brosen, S. Benhamou, C. Bouchardy, G. R. Wilkinson, P. Dayer, and J. A. Goldstein. A novel transversion in the intron 5 donor splice junction of CYP2C19 and a sequence polymorphism in exon 3 contribute to the poor metabolizer phenotype for the anticonvulsant drug S-mephenytoin. J. Pharmacol. Exp. Ther. 290:635-640 (1999).
    • (1999) J. Pharmacol. Exp. Ther. , vol.290 , pp. 635-640
    • Ibeanu, G.C.1    Blaisdell, J.2    Gerguson, R.J.3    Ghanayem, B.I.4    Brosen, K.5    Benhamou, S.6    Bouchardy, C.7    Wilkinson, G.R.8    Dayer, P.9    Goldstein, J.A.10
  • 12
    • 0023650353 scopus 로고
    • cDNA and amino acid sequences of two members of the human P450IIC gene subfamily
    • S. Kimura, J. Pastewka, H. V. Gelboin, and F. J. Gonzalez. cDNA and amino acid sequences of two members of the human P450IIC gene subfamily. Nucleic Acids Res. 15:10053-10054 (1987).
    • (1987) Nucleic Acids Res. , vol.15 , pp. 10053-10054
    • Kimura, S.1    Pastewka, J.2    Gelboin, H.V.3    Gonzalez, F.J.4
  • 13
    • 0035916224 scopus 로고    scopus 로고
    • Identification of human CYP2C19 residues that confer S-mephenytoin 4′-hydroxylation activity to CYP2C9
    • C.-C. Tsao, M. R. Wester, B. Ghanayem, S. J. Coulter, B. Chanas, E. F. Johnson, and J. A. Goldstein. Identification of human CYP2C19 residues that confer S-mephenytoin 4′-hydroxylation activity to CYP2C9. Biochemistry 40:1937-1944 (2001).
    • (2001) Biochemistry , vol.40 , pp. 1937-1944
    • Tsao, C.-C.1    Wester, M.R.2    Ghanayem, B.3    Coulter, S.J.4    Chanas, B.5    Johnson, E.F.6    Goldstein, J.A.7
  • 14
    • 0033970047 scopus 로고    scopus 로고
    • Mammalian microsomal cytochrome P450 monooxygenase: Structural adaptations for membrane binding and functional diversity
    • P. A. Williams, J. Cosme, V. Sridhar, E. F. Johnson, and D. E. McRee. Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity. Mol. Cell 5:121-131 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 121-131
    • Williams, P.A.1    Cosme, J.2    Sridhar, V.3    Johnson, E.F.4    McRee, D.E.5
  • 16
    • 0030599010 scopus 로고    scopus 로고
    • A fast flexible docking method using an incremental construction algorithm
    • M. Rarey, B. Kramer, T. Lengauer, and G. Klebe. A fast flexible docking method using an incremental construction algorithm. J. Mol. Biol. 261:470-489 (1996).
    • (1996) J. Mol. Biol. , vol.261 , pp. 470-489
    • Rarey, M.1    Kramer, B.2    Lengauer, T.3    Klebe, G.4
  • 17
    • 0035025191 scopus 로고    scopus 로고
    • DOCK 4.0: Search strategies for automated molecular docking of flexible molecule databases
    • T. J. Ewing. DOCK 4.0: search strategies for automated molecular docking of flexible molecule databases. J. Comput. Aided Mol. Des. 15:411-428 (2001).
    • (2001) J. Comput. Aided Mol. Des. , vol.15 , pp. 411-428
    • Ewing, T.J.1
  • 18
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • G. Jones, P. Willet, R. C. Glen, A. R. Leach, and R. Taylor. Development and validation of a genetic algorithm for flexible docking. J. Mol. Biol. 267:727-748 (1997).
    • (1997) J. Mol. Biol. , vol.267 , pp. 727-748
    • Jones, G.1    Willet, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 19
    • 0031934315 scopus 로고    scopus 로고
    • Molecular modeling of human CYP2C subfamily enzymes CYP2C9 and CYP2C19: Rationalization of substrate specificity and site-directed mutagenesis experiments in the CYP2C subfamily
    • D. F. V. Lewis, M. Dickins, R. J. Weaver, P. J. Eddershaw, P. S. Goldfarb, and M. H. Tarbit. Molecular modeling of human CYP2C subfamily enzymes CYP2C9 and CYP2C19: rationalization of substrate specificity and site-directed mutagenesis experiments in the CYP2C subfamily. Xenobiotica 28:235-268 (1998).
    • (1998) Xenobiotica , vol.28 , pp. 235-268
    • Lewis, D.F.V.1    Dickins, M.2    Weaver, R.J.3    Eddershaw, P.J.4    Goldfarb, P.S.5    Tarbit, M.H.6
  • 20
    • 0032744799 scopus 로고    scopus 로고
    • Homology modeling and substrate binding study of human CYP2C18 and CYP2C19 enzymes
    • V. A. Payne, Y.-T. Chang, and G. H. Loew. Homology modeling and substrate binding study of human CYP2C18 and CYP2C19 enzymes. Proteins 37:204-217 (1999).
    • (1999) Proteins , vol.37 , pp. 204-217
    • Payne, V.A.1    Chang, Y.-T.2    Loew, G.H.3
  • 21
    • 0035935677 scopus 로고    scopus 로고
    • Analysis of selective regions in the active sites of human cytochromes P450, 2C8, 2C9, 2C18 and 2C19 homology models using GRID/CPCA
    • M. Ridderström, I. Zamora, O. Fjellström, and T. B. Andersson. Analysis of selective regions in the active sites of human cytochromes P450, 2C8, 2C9, 2C18 and 2C19 homology models using GRID/CPCA. J. Med. Chem. 44:4072-4081 (2001).
    • (2001) J. Med. Chem. , vol.44 , pp. 4072-4081
    • Ridderström, M.1    Zamora, I.2    Fjellström, O.3    Andersson, T.B.4
  • 22
    • 0037145065 scopus 로고    scopus 로고
    • Modeling human cytochromes P450 involved in drug metabolism from the CYP2C5 crystallographic template
    • D. F. V. Lewis. Modeling human cytochromes P450 involved in drug metabolism from the CYP2C5 crystallographic template. J. Inorg. Biochem. 91:502-514 (2002).
    • (2002) J. Inorg. Biochem. , vol.91 , pp. 502-514
    • Lewis, D.F.V.1
  • 23
    • 0037046521 scopus 로고    scopus 로고
    • Development of a combined protein and pharmacophore model for cytochrome P450 2C9
    • M. J. de Groot, A. A. Alex, and B. C. Jones. Development of a combined protein and pharmacophore model for cytochrome P450 2C9. J. Med. Chem. 45:1983-1993 (2002).
    • (2002) J. Med. Chem. , vol.45 , pp. 1983-1993
    • De Groot, M.J.1    Alex, A.A.2    Jones, B.C.3
  • 24
    • 0034465184 scopus 로고    scopus 로고
    • An automatic homology modeling method consisting of database searches and simulated annealing
    • K. Ogata and H. Umeyama. An automatic homology modeling method consisting of database searches and simulated annealing. J. Mol. Graphics Mod. 18:258-272 (2000).
    • (2000) J. Mol. Graphics Mod. , vol.18 , pp. 258-272
    • Ogata, K.1    Umeyama, H.2
  • 26
    • 84986468608 scopus 로고
    • An approach to computing electrostatic charges for molecules
    • U. C. Singh and P. A. Kollman. An approach to computing electrostatic charges for molecules. J. Comput. Chem. 5:129-145 (1984).
    • (1984) J. Comput. Chem. , vol.5 , pp. 129-145
    • Singh, U.C.1    Kollman, P.A.2
  • 28
    • 0031138076 scopus 로고    scopus 로고
    • CAMDAS: An automated conformational analysis system using molecular dynamics
    • H. Tsujishita and S. Hirono. CAMDAS: an automated conformational analysis system using molecular dynamics. J. Comput. Aided Mol. Des. 11:305-315 (1997).
    • (1997) J. Comput. Aided Mol. Des. , vol.11 , pp. 305-315
    • Tsujishita, H.1    Hirono, S.2
  • 29
    • 0037571112 scopus 로고    scopus 로고
    • Merck molecular force field. I. Basis, form, scope, parameterization, and performance of MMFF94
    • T. A. Halgren. Merck molecular force field. I. Basis, form, scope, parameterization, and performance of MMFF94. J. Comput. Chem. 17:490-519 (1996).
    • (1996) J. Comput. Chem. , vol.17 , pp. 490-519
    • Halgren, T.A.1
  • 30
    • 0033545622 scopus 로고    scopus 로고
    • A general and fast scoring function for protein-ligand interactions: A simplified potential approach
    • I. Muegge and Y. C. Martin. A general and fast scoring function for protein-ligand interactions: a simplified potential approach. J. Med. Chem. 42:791-804 (1999).
    • (1999) J. Med. Chem. , vol.42 , pp. 791-804
    • Muegge, I.1    Martin, Y.C.2
  • 32
    • 0031226772 scopus 로고    scopus 로고
    • Empirical scoring functions: I. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes
    • M. D. Eldridge, C. W. Murray, T. R. Auton, G. V. Paolini, and R. P. Mee. Empirical scoring functions: I. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes. J. Comput. Aided Mol. Des. 11:425-445 (1997).
    • (1997) J. Comput. Aided Mol. Des. , vol.11 , pp. 425-445
    • Eldridge, M.D.1    Murray, C.W.2    Auton, T.R.3    Paolini, G.V.4    Mee, R.P.5
  • 33
    • 0033576680 scopus 로고    scopus 로고
    • Consensus scoring: A method for obtaining improved hit rates from docking databases of three-dimensional structures into proteins
    • P. S. Charifson, J. J. Corkery, M. A. Murcko, and W. P. Walters. Consensus scoring: a method for obtaining improved hit rates from docking databases of three-dimensional structures into proteins. J. Med. Chem. 42:5100-5109 (1999).
    • (1999) J. Med. Chem. , vol.42 , pp. 5100-5109
    • Charifson, P.S.1    Corkery, J.J.2    Murcko, M.A.3    Walters, W.P.4
  • 36
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • J. P. Ryckaert, G. Cicotti, and H. J. C. Berensden. Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J. Comput. Phys. 23:327-341 (1977).
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Cicotti, G.2    Berensden, H.J.C.3
  • 37
    • 0026542989 scopus 로고
    • Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences
    • O. Gotoh. Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences. J. Biol. Chem. 267:83-90 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 83-90
    • Gotoh, O.1
  • 38
    • 0037672866 scopus 로고    scopus 로고
    • Structure of a substrate complex of mammalian cytochrome P450 2C5 at 2.3 A resolution: Evidence for multiple substrate binding modes
    • M. R. Wester, E. F. Johnson, C. Marques-Soares, P. M. Dansette, D. Mansuy, and C. D. Stout. Structure of a substrate complex of mammalian cytochrome P450 2C5 at 2.3 A resolution: evidence for multiple substrate binding modes. Biochemistry 42:6370-6379 (2003).
    • (2003) Biochemistry , vol.42 , pp. 6370-6379
    • Wester, M.R.1    Johnson, E.F.2    Marques-Soares, C.3    Dansette, P.M.4    Mansuy, D.5    Stout, C.D.6
  • 39
    • 0042265520 scopus 로고    scopus 로고
    • Crystal structure of human cytochrome P450 2C9 with bound warfarin
    • P. A. Williams, J. Cosme, A. Ward, H. C. Angove, D. M. Vinkovi, and H. Jhoti. Crystal structure of human cytochrome P450 2C9 with bound warfarin. Nature 424:464-468 (2003).
    • (2003) Nature , vol.424 , pp. 464-468
    • Williams, P.A.1    Cosme, J.2    Ward, A.3    Angove, H.C.4    Vinkovi, D.M.5    Jhoti, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.