메뉴 건너뛰기




Volumn 32, Issue 11, 2004, Pages 1218-1229

Structural analysis of CYP2C9 and CYP2C5 and an evaluation of commonly used molecular modeling techniques

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CYTOCHROME P450 2C5; CYTOCHROME P450 2C9; CYTOCHROME P450 ISOENZYME; UNCLASSIFIED DRUG;

EID: 6944226372     PISSN: 00909556     EISSN: None     Source Type: Journal    
DOI: 10.1124/dmd.32.11.1218     Document Type: Article
Times cited : (26)

References (38)
  • 1
    • 0035065393 scopus 로고    scopus 로고
    • Competitive CYP2C9 inhibitors: Enzyme inhibition studies, protein homology modeling and three-dimensional quantitative structure-activity relationship analysis
    • Afzelius L, Zamora I, Ridderstrom M, Andersson TB, Karlen A, and Masimirembwa CM (2001) Competitive CYP2C9 inhibitors: enzyme inhibition studies, protein homology modeling and three-dimensional quantitative structure-activity relationship analysis. Mol Pharmacol 59: 909-919.
    • (2001) Mol Pharmacol , vol.59 , pp. 909-919
    • Afzelius, L.1    Zamora, I.2    Ridderstrom, M.3    Andersson, T.B.4    Karlen, A.5    Masimirembwa, C.M.6
  • 2
    • 0027310371 scopus 로고
    • Generating optimal linear PLS estimations (GOLPE): An advanced chemometric tool for handling 3D-QSAR problems
    • Baroni M, Cruciani G, Costantino G, Riganelli D, Valigi R, and Clementi S (1993) Generating optimal linear PLS estimations (GOLPE): an advanced chemometric tool for handling 3D-QSAR problems. Quant Struct-Act Relat 12:9-20.
    • (1993) Quant Struct-Act Relat , vol.12 , pp. 9-20
    • Baroni, M.1    Cruciani, G.2    Costantino, G.3    Riganelli, D.4    Valigi, R.5    Clementi, S.6
  • 6
    • 0034724310 scopus 로고    scopus 로고
    • Crystal structures of ligand complexes of P450eryF exhibiting homotropic cooperativity
    • Cupp-Vickery J, Anderson R, and Hatziris Z (2000) Crystal structures of ligand complexes of P450eryF exhibiting homotropic cooperativity. Proc Natl Acad Sci USA 97:3050-3055.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3050-3055
    • Cupp-Vickery, J.1    Anderson, R.2    Hatziris, Z.3
  • 7
    • 0010621578 scopus 로고    scopus 로고
    • Molecular modeling of mammalian cytochrome P450
    • Dai R, Pincus MR, and Friedman FK (2000) Molecular modeling of mammalian cytochrome P450. Cell Mol Life Sci 57:487-499.
    • (2000) Cell Mol Life Sci , vol.57 , pp. 487-499
    • Dai, R.1    Pincus, M.R.2    Friedman, F.K.3
  • 8
    • 1842484814 scopus 로고    scopus 로고
    • Assessment of arginine 97 and lysine 72 as determinants of substrate specificity in cytochrome P450 2C9 (CYP2C9)
    • Davies C, Witham K, Scott JR, Pearson A, DeVoss JJ, Graham SE, and Gillam EMJ (2004) Assessment of arginine 97 and lysine 72 as determinants of substrate specificity in cytochrome P450 2C9 (CYP2C9). Drug Metab Dispos 32:431-436.
    • (2004) Drug Metab Dispos , vol.32 , pp. 431-436
    • Davies, C.1    Witham, K.2    Scott, J.R.3    Pearson, A.4    DeVoss, J.J.5    Graham, S.E.6    Gillam, E.M.J.7
  • 9
    • 0037046521 scopus 로고    scopus 로고
    • Development of a combined protein and pharmacophore model for cytochrome P450 2C9
    • de Groot MJ, Alex AA, and Jones BC (2002) Development of a combined protein and pharmacophore model for cytochrome P450 2C9. J Med Chem 45:1983-1993.
    • (2002) J Med Chem , vol.45 , pp. 1983-1993
    • De Groot, M.J.1    Alex, A.A.2    Jones, B.C.3
  • 11
    • 6944222574 scopus 로고
    • Ph.D. thesis, University of California
    • Giammona DA (1984), Ph.D. thesis, University of California.
    • (1984)
    • Giammona, D.A.1
  • 12
    • 0021871375 scopus 로고
    • A computational procedure for determining energetically favorable binding sites on biologically important macromolecules
    • Goodford PJ (1985) A computational procedure for determining energetically favorable binding sites on biologically important macromolecules. J Med Chem 28:849-857.
    • (1985) J Med Chem , vol.28 , pp. 849-857
    • Goodford, P.J.1
  • 13
    • 0029892263 scopus 로고    scopus 로고
    • P450s: Structural similarities and functional differences
    • Graham-Lorence S and Peterson JA (1996) P450s: structural similarities and functional differences. FASEB J 10:206-214.
    • (1996) FASEB J , vol.10 , pp. 206-214
    • Graham-Lorence, S.1    Peterson, J.A.2
  • 14
    • 0028267490 scopus 로고
    • Crystal structure and refinement of cytochrome P450terp at 2.3 a resolution
    • Hasemann CA, Ravichandran KG, Peterson JA, and Deisenhofer J (1994) Crystal structure and refinement of cytochrome P450terp at 2.3 A resolution. J Mol Biol 236:1169-1185.
    • (1994) J Mol Biol , vol.236 , pp. 1169-1185
    • Hasemann, C.A.1    Ravichandran, K.G.2    Peterson, J.A.3    Deisenhofer, J.4
  • 15
    • 0032542015 scopus 로고    scopus 로고
    • Identification of amino acid substitutions that confer a high affinity for sulfaphenazole binding and a high catalytic efficiency for warfarin metabolism to P450 2C19
    • Jung F, Griffin KJ, Song W, Richardson TH, Yang M, and Johnson EF (1998) Identification of amino acid substitutions that confer a high affinity for sulfaphenazole binding and a high catalytic efficiency for warfarin metabolism to P450 2C19. Biochemistry 37:16270-16279.
    • (1998) Biochemistry , vol.37 , pp. 16270-16279
    • Jung, F.1    Griffin, K.J.2    Song, W.3    Richardson, T.H.4    Yang, M.5    Johnson, E.F.6
  • 18
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, and Thornton JM (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Ctystallogr 26:283-291.
    • (1993) J Appl Ctystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 19
    • 0034525310 scopus 로고    scopus 로고
    • Modeling human cytochromes P450 for evaluating drug metabolism: An update
    • Lewis DF (2000) Modeling human cytochromes P450 for evaluating drug metabolism: an update. Drug Metab Drug Interact 16:307-324.
    • (2000) Drug Metab Drug Interact , vol.16 , pp. 307-324
    • Lewis, D.F.1
  • 20
    • 0036267032 scopus 로고    scopus 로고
    • Homology modelling of human CYP2 family enzymes based on the CYP2C5 crystal structure
    • Lewis DF (2002) Homology modelling of human CYP2 family enzymes based on the CYP2C5 crystal structure. Xenobiotica 32:305-323.
    • (2002) Xenobiotica , vol.32 , pp. 305-323
    • Lewis, D.F.1
  • 21
    • 0031934315 scopus 로고    scopus 로고
    • Molecular modelling of human CYP2C subfamily enzymes CYP2C9 and CYP2C19: Rationalization of substrate specificity and site-directed mutagenesis experiments in the CYP2C subfamily
    • Lewis DF, Dickins M, Weaver RJ, Eddershaw PJ, Goldfarb PS, and Tarbit MH (1998) Molecular modelling 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) Xenobiotica , vol.28 , pp. 235-268
    • Lewis, D.F.1    Dickins, M.2    Weaver, R.J.3    Eddershaw, P.J.4    Goldfarb, P.S.5    Tarbit, M.H.6
  • 22
    • 0037228099 scopus 로고    scopus 로고
    • Substrate selectivity of human cytochrome P450 2C9: Importance of residues 476, 365 and 114 in recognition of diclofenac and sulfaphenazole and in mechanism-based inactivation by tienilic acid
    • Melet A, Assrir N, Jean P, Pilar Lopez-Garcia M, Marques-Soares C, Jaouen M, Dansette PM, Sari MA, and Mansuy D (2003) Substrate selectivity of human cytochrome P450 2C9: importance of residues 476, 365 and 114 in recognition of diclofenac and sulfaphenazole and in mechanism-based inactivation by tienilic acid. Arch Biochem Biophys 409:80-91.
    • (2003) Arch Biochem Biophys , vol.409 , pp. 80-91
    • Melet, A.1    Assrir, N.2    Jean, P.3    Pilar Lopez-Garcia, M.4    Marques-Soares, C.5    Jaouen, M.6    Dansette, P.M.7    Sari, M.A.8    Mansuy, D.9
  • 23
    • 0035984571 scopus 로고    scopus 로고
    • Oxidizing species in the mechanism of cytochrome P450
    • Ortiz de Montellano PR and De Voss JJ (2002) Oxidizing species in the mechanism of cytochrome P450. Nat Prod Rep 19:477-493.
    • (2002) Nat Prod Rep , vol.19 , pp. 477-493
    • Ortiz De Montellano, P.R.1    De Voss, J.J.2
  • 24
    • 0032742735 scopus 로고    scopus 로고
    • Homology modeling and substrate binding study of human CYP2C9 enzyme
    • Payne VA, Chang Y-T, and Loew GH (1999) Homology modeling and substrate binding study of human CYP2C9 enzyme. Proteins Struct Funct Genet 37:176-190.
    • (1999) Proteins Struct Funct Genet , vol.37 , pp. 176-190
    • Payne, V.A.1    Chang, Y.-T.2    Loew, G.H.3
  • 25
    • 0032530250 scopus 로고    scopus 로고
    • A close family resemblance: The importance of structure in understanding cytochromes P450
    • Peterson JA and Graham SE (1998) A close family resemblance: the importance of structure in understanding cytochromes P450. Structure 6:1079-1085.
    • (1998) Structure , vol.6 , pp. 1079-1085
    • Peterson, J.A.1    Graham, S.E.2
  • 26
    • 0022919721 scopus 로고
    • Crystal structure of substrate-free Pseudomonas putida cytochrome P-450
    • Poulos TL, Finzel BC, and Howard AJ (1986) Crystal structure of substrate-free Pseudomonas putida cytochrome P-450. Biochemistry 25:5314-5322.
    • (1986) Biochemistry , vol.25 , pp. 5314-5322
    • Poulos, T.L.1    Finzel, B.C.2    Howard, A.J.3
  • 28
    • 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
    • Ridderstrom M, Zamora I, Fjellstrom O, and Andersson TB (2001 ) 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) J Med Chem , vol.44 , pp. 4072-4081
    • Ridderstrom, M.1    Zamora, I.2    Fjellstrom, O.3    Andersson, T.B.4
  • 29
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equation of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert J-R, Ciccotti G, and Berendsen HJC (1977) Numerical integration of the cartesian equation of motion of a system with constraints: molecular dynamics of n-alkanes. J Comput Phys 23:1977.
    • (1977) J Comput Phys , vol.23 , pp. 1977
    • Ryckaert, J.-R.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 32
    • 0031457404 scopus 로고    scopus 로고
    • Use of homology modeling in conjunction with site-directed mutagenesis for analysis of structure-function relationships of mammalian cytochromes P450
    • Szklarz GD and Halpert JR (1997) Use of homology modeling in conjunction with site-directed mutagenesis for analysis of structure-function relationships of mammalian cytochromes P450. Life Sci 61:2507-2520.
    • (1997) Life Sci , vol.61 , pp. 2507-2520
    • Szklarz, G.D.1    Halpert, J.R.2
  • 33
    • 0037672866 scopus 로고    scopus 로고
    • Structure of a substrate complex of mammalian cytochrome P450 2C5 at 2.3 Å resolution: Evidence for multiple substrate binding modes
    • Wester MR, Johnson EF, Marques-Soares C, Dansette PM, Mansuy D, and Stout CD (2003a) Structure of a substrate complex of mammalian cytochrome P450 2C5 at 2.3 Å resolution: evidence for multiple substrate binding modes. Biochemistry 42:6370-6379.
    • (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
  • 34
    • 0042573727 scopus 로고    scopus 로고
    • Structure of mammalian cytochrome P450 2C5 complexed with diciofenac at 2.1 Å resolution: Evidence for an induced fit model of substrate binding
    • Wester MR, Johnson EF, Marques-Soares C, Dijols S, Dansette PM, Mansuy D, and Stout CD (2003b) Structure of mammalian cytochrome P450 2C5 complexed with diciofenac at 2.1 Å resolution: evidence for an induced fit model of substrate binding. Biochemistry 42:9335-9345.
    • (2003) Biochemistry , vol.42 , pp. 9335-9345
    • Wester, M.R.1    Johnson, E.F.2    Marques-Soares, C.3    Dijols, S.4    Dansette, P.M.5    Mansuy, D.6    Stout, C.D.7
  • 35
    • 0033970047 scopus 로고    scopus 로고
    • Mammalian microsomal cytochrome P450 monooxygenase: Structural adaptations for membrane binding and functional diversity
    • Williams PA, Cosme J, Sridhar V, Johnson EF, and McRee DE (2000) Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity. Mol Cell 5:121-131.
    • (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
  • 37
    • 0033614004 scopus 로고    scopus 로고
    • Asparagine and glutamine: Using hydrogen atom contacts in the choice of side-chain amide orientation
    • Word J, Lovell SC, Richardson JS, and Richardson DC (1999) Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation. J Mol Biol 285:1733-1747.
    • (1999) J Mol Biol , vol.285 , pp. 1733-1747
    • Word, J.1    Lovell, S.C.2    Richardson, J.S.3    Richardson, D.C.4
  • 38
    • 0038440502 scopus 로고    scopus 로고
    • Predicting drug metabolism: A site of metabolism prediction tool applied to the cytochrome P450 2C9
    • Zamora I, Afzelius L, and Cruciani G (2003) Predicting drug metabolism: a site of metabolism prediction tool applied to the cytochrome P450 2C9. J Med Chem 46:2313-2324.
    • (2003) J Med Chem , vol.46 , pp. 2313-2324
    • Zamora, I.1    Afzelius, L.2    Cruciani, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.