메뉴 건너뛰기




Volumn 78, Issue 4, 2009, Pages 406-413

Evaluation of the binding orientations of testosterone in the active site of homology models for CYP2C11 and CYP2C13

Author keywords

CYP binding site; CYP2C; Homology modeling; Substrate docking; Testosterone metabolism

Indexed keywords

CYTOCHROME P450; CYTOCHROME P450 2C11; CYTOCHROME P450 2C13; TESTOSTERONE; UNCLASSIFIED DRUG;

EID: 67349240434     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2009.04.020     Document Type: Article
Times cited : (23)

References (31)
  • 1
    • 0034970549 scopus 로고    scopus 로고
    • Uncommon P450-catalyzed reactions
    • Guengerich F.P. Uncommon P450-catalyzed reactions. Curr Drug Metab 2 (2001) 93-115
    • (2001) Curr Drug Metab , vol.2 , pp. 93-115
    • Guengerich, F.P.1
  • 2
    • 0036223831 scopus 로고    scopus 로고
    • Summary of information on human CYP enzymes: human P450 metabolism data
    • Rendic S. Summary of information on human CYP enzymes: human P450 metabolism data. Drug Metab Rev 34 (2002) 83-448
    • (2002) Drug Metab Rev , vol.34 , pp. 83-448
    • Rendic, S.1
  • 3
    • 0023796707 scopus 로고
    • Feminization of rat hepatic P-450 expression by cisplatin-Evidence for pertubations in the hormonal regulation of steroid-metabolizing enzymes
    • Leblanc G.A., and Waxman D.J. Feminization of rat hepatic P-450 expression by cisplatin-Evidence for pertubations in the hormonal regulation of steroid-metabolizing enzymes. J Biol Chem 263 (1988) 15732-15739
    • (1988) J Biol Chem , vol.263 , pp. 15732-15739
    • Leblanc, G.A.1    Waxman, D.J.2
  • 4
    • 0023411808 scopus 로고
    • Purification of human liver cytochrome P-450 catalyzing testosterone 6β-hydroxylation
    • Kawano S., Karnataki T., Yasumori T., Yamazoe Y., and Keto R. Purification of human liver cytochrome P-450 catalyzing testosterone 6β-hydroxylation. J Biochem 102 (1987) 493-501
    • (1987) J Biochem , vol.102 , pp. 493-501
    • Kawano, S.1    Karnataki, T.2    Yasumori, T.3    Yamazoe, Y.4    Keto, R.5
  • 5
    • 0031260323 scopus 로고    scopus 로고
    • Progesterone and testosterone metabolism by cytochromes 2C19, 2C9 and 3A4 in human liver microsomes
    • Yamazaki H., and Shimada T. Progesterone and testosterone metabolism by cytochromes 2C19, 2C9 and 3A4 in human liver microsomes. Arch Biochem Biophys 346 (1997) 161-169
    • (1997) Arch Biochem Biophys , vol.346 , pp. 161-169
    • Yamazaki, H.1    Shimada, T.2
  • 6
    • 0020634273 scopus 로고
    • Testosterone metabolism by cytochrome P-450 isozymes RLM3 and RLM5 and by microsomes. Metabolite identification
    • Cheng K.C., and Schenkman J.B. Testosterone metabolism by cytochrome P-450 isozymes RLM3 and RLM5 and by microsomes. Metabolite identification. J Biol Chem 258 (1983) 11738-11744
    • (1983) J Biol Chem , vol.258 , pp. 11738-11744
    • Cheng, K.C.1    Schenkman, J.B.2
  • 7
    • 0033970047 scopus 로고    scopus 로고
    • Mammalian microsomal cytochrome p450 monooxygenase: structural adaptations for membrane binding and functional diversity
    • Williams P.A., Cosme J., Sridhar V., Johnson E.F., and McRee D.E. Mammalian microsomal cytochrome p450 monooxygenase: structural adaptations for membrane binding and functional diversity. Mol Cell 5 (2000) 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
  • 8
    • 0033569516 scopus 로고    scopus 로고
    • Pharmacogenomics: translating functional genomics to rational therapeutics
    • Evans W.E., and Relling M.V. Pharmacogenomics: translating functional genomics to rational therapeutics. Science 286 (1999) 487-491
    • (1999) Science , vol.286 , pp. 487-491
    • Evans, W.E.1    Relling, M.V.2
  • 9
    • 4143143372 scopus 로고    scopus 로고
    • The structure of human cytochrome p450 2c9 complexed with flurbiprofen at 2.0-a resolution
    • Wester M.R., Yano J.K., Schoch G.A., Yang C., Griffin K.J., Stout C.D., et al. The structure of human cytochrome p450 2c9 complexed with flurbiprofen at 2.0-a resolution. J Biol Chem 279 (2004) 35630-35637
    • (2004) J Biol Chem , vol.279 , pp. 35630-35637
    • Wester, M.R.1    Yano, J.K.2    Schoch, G.A.3    Yang, C.4    Griffin, K.J.5    Stout, C.D.6
  • 10
    • 3442896773 scopus 로고    scopus 로고
    • Crystal structures of human cytochrome P450 3A4 bound to metyrapone and progesterone
    • Williams P.A., Cosme J., Vinkovic D.M., Ward A., Angove H.C., Day P.J., et al. Crystal structures of human cytochrome P450 3A4 bound to metyrapone and progesterone. Science 305 (2004) 683-686
    • (2004) Science , vol.305 , pp. 683-686
    • Williams, P.A.1    Cosme, J.2    Vinkovic, D.M.3    Ward, A.4    Angove, H.C.5    Day, P.J.6
  • 11
    • 33748802003 scopus 로고    scopus 로고
    • From the cover: structural basis for ligand promiscuity in cytochrome P450 3A4
    • Ekroos M., and Sjogren T. From the cover: structural basis for ligand promiscuity in cytochrome P450 3A4. Proc Natl Acad Sci USA 103 (2006) 13682-13687
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13682-13687
    • Ekroos, M.1    Sjogren, T.2
  • 12
    • 47749092044 scopus 로고    scopus 로고
    • Determinants of cytochrome P450 2C8 substrate binding: structures of complexes with montelukast, troglitazone, felodipine, and 9-cis-retinoic acid
    • Schoch G.A., Yano J.K., Sansen S., Dansette P.M., Stout C.D., and Johnson E.F. Determinants of cytochrome P450 2C8 substrate binding: structures of complexes with montelukast, troglitazone, felodipine, and 9-cis-retinoic acid. J Biol Chem 283 (2008) 17227-17237
    • (2008) J Biol Chem , vol.283 , pp. 17227-17237
    • Schoch, G.A.1    Yano, J.K.2    Sansen, S.3    Dansette, P.M.4    Stout, C.D.5    Johnson, E.F.6
  • 14
    • 1542364450 scopus 로고    scopus 로고
    • Structure of human microsomal cytochrome P450 2C8: evidence for a peripheral fatty acid binding site
    • Schoch G.A., Yano J.K., Wester M.R., Griffin K.J., Stout C.D., and Johnson E.F. Structure of human microsomal cytochrome P450 2C8: evidence for a peripheral fatty acid binding site. J Biol Chem 279 (2004) 9497-9503
    • (2004) J Biol Chem , vol.279 , pp. 9497-9503
    • Schoch, G.A.1    Yano, J.K.2    Wester, M.R.3    Griffin, K.J.4    Stout, C.D.5    Johnson, E.F.6
  • 15
    • 3042519587 scopus 로고    scopus 로고
    • Cytochrome P450: what have we learned and what are the future issues?
    • Guengerich F.P. Cytochrome P450: what have we learned and what are the future issues?. Drug Metab Rev 36 (2004) 159-197
    • (2004) Drug Metab Rev , vol.36 , pp. 159-197
    • Guengerich, F.P.1
  • 16
    • 34250346536 scopus 로고    scopus 로고
    • Multiple sequential steps involved in the binding of inhibitors to cytochrome P-450 3A4
    • Isin E.M., and Guengerich F.P. Multiple sequential steps involved in the binding of inhibitors to cytochrome P-450 3A4. J Biol Chem 282 (2007) 6863-6874
    • (2007) J Biol Chem , vol.282 , pp. 6863-6874
    • Isin, E.M.1    Guengerich, F.P.2
  • 17
    • 38549097071 scopus 로고    scopus 로고
    • The universal protein resource (UniProt)
    • The UniProt Consortium. The universal protein resource (UniProt). Nucl Acids Res 36 (2008) D190-D195
    • (2008) Nucl Acids Res , vol.36
    • The UniProt Consortium1
  • 20
    • 0036368570 scopus 로고    scopus 로고
    • Complete protein structure determination using backbone residual dipolar couplings and sidechain rotamer predication
    • Andrec M., Harano Y., Jacobson M.P., Friesner R.A., and Levy R.M. Complete protein structure determination using backbone residual dipolar couplings and sidechain rotamer predication. J Struct Funct Genom 2 (2002) 103-111
    • (2002) J Struct Funct Genom , vol.2 , pp. 103-111
    • Andrec, M.1    Harano, Y.2    Jacobson, M.P.3    Friesner, R.A.4    Levy, R.M.5
  • 21
    • 33751544804 scopus 로고    scopus 로고
    • Identification of binding sites of non-i-helix water molecules in mammalian cytochromes P450
    • Locuson C.W., and Tracy T.S. Identification of binding sites of non-i-helix water molecules in mammalian cytochromes P450. Drug Metab Dispos 34 (2006) 1954-1957
    • (2006) Drug Metab Dispos , vol.34 , pp. 1954-1957
    • Locuson, C.W.1    Tracy, T.S.2
  • 22
    • 36649014061 scopus 로고    scopus 로고
    • Improved methods for side chain and loop predictions via the protein local optimization program: variable dielectric model for implicitly improving the treatment of polarization effects
    • Zhu K., Shirts M.A., and Friesner R.A. Improved methods for side chain and loop predictions via the protein local optimization program: variable dielectric model for implicitly improving the treatment of polarization effects. J Chem Theory Comput 3 (2007) 2108-2119
    • (2007) J Chem Theory Comput , vol.3 , pp. 2108-2119
    • Zhu, K.1    Shirts, M.A.2    Friesner, R.A.3
  • 23
    • 0027995683 scopus 로고
    • Detection, delineation, measurement and display of cavities in macromolecular structures
    • Kleywegt G.J., and Jones T.A. Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Cryst Sec D 50 (1994) 178-185
    • (1994) Acta Cryst Sec D , vol.50 , pp. 178-185
    • Kleywegt, G.J.1    Jones, T.A.2
  • 24
    • 12144289984 scopus 로고    scopus 로고
    • Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy
    • Friesner R.A., Banks J.L., Murphy R.B., Halgren T.A., Klicic J.J., Mainz D.T., et al. Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy. J Med Chem 47 (2004) 1739-1749
    • (2004) J Med Chem , vol.47 , pp. 1739-1749
    • Friesner, R.A.1    Banks, J.L.2    Murphy, R.B.3    Halgren, T.A.4    Klicic, J.J.5    Mainz, D.T.6
  • 25
    • 31544450787 scopus 로고    scopus 로고
    • Novel procedure for modeling ligand/receptor induced fit effects
    • Sherman W., Day T., Jacobson M.P., Friesner R.A., and Farid R. Novel procedure for modeling ligand/receptor induced fit effects. J Med Chem 49 (2006) 534-553
    • (2006) J Med Chem , vol.49 , pp. 534-553
    • Sherman, W.1    Day, T.2    Jacobson, M.P.3    Friesner, R.A.4    Farid, R.5
  • 26
    • 37349085453 scopus 로고    scopus 로고
    • A flexible approach to induced fit docking
    • Nabuurs S.B., Wagener M., and de Vlieg J. A flexible approach to induced fit docking. J Med Chem 50 (2007) 6507-6518
    • (2007) J Med Chem , vol.50 , pp. 6507-6518
    • Nabuurs, S.B.1    Wagener, M.2    de Vlieg, J.3
  • 27
    • 0030954347 scopus 로고    scopus 로고
    • Cytochrome P450 2C11: E. coli expression, purification, functional characterization, and mechanism-based inactivation of the enzyme
    • Licas-Coles E., He K., Yin H., and Correia M.A. Cytochrome P450 2C11: E. coli expression, purification, functional characterization, and mechanism-based inactivation of the enzyme. Arch Biochem Biophys 338 (1997) 35-42
    • (1997) Arch Biochem Biophys , vol.338 , pp. 35-42
    • Licas-Coles, E.1    He, K.2    Yin, H.3    Correia, M.A.4
  • 28
    • 0021282412 scopus 로고
    • Metabolism of progesterone and estradiol by microsomes and purified cytochrome P-450 RLM3 and RLM5
    • Cheng K.C., and Schenkman J.B. Metabolism of progesterone and estradiol by microsomes and purified cytochrome P-450 RLM3 and RLM5. Drug Metab Dispos 12 (1984) 222-234
    • (1984) Drug Metab Dispos , vol.12 , pp. 222-234
    • Cheng, K.C.1    Schenkman, J.B.2
  • 29
    • 0034723195 scopus 로고    scopus 로고
    • Engineering microsomal cytochrome P-450 2C5 to be a soluble, monomeric enzyme mutations that alter aggregation, phospholipids dependence of membrane binding and catalysis
    • Cosme J., and John E.F. Engineering microsomal cytochrome P-450 2C5 to be a soluble, monomeric enzyme mutations that alter aggregation, phospholipids dependence of membrane binding and catalysis. J Biol Chem 275 (2000) 2549-2553
    • (2000) J Biol Chem , vol.275 , pp. 2549-2553
    • Cosme, J.1    John, E.F.2
  • 30
    • 25844447810 scopus 로고    scopus 로고
    • Thermal equilibrium of high- and low-spin forms of cytochrome P450 BM-s: repositioning of the substrate
    • Jovanovic T., Farid R., Friesner R.A., and McDermott A.E. Thermal equilibrium of high- and low-spin forms of cytochrome P450 BM-s: repositioning of the substrate. J Am Chem Soc 127 (2005) 13548-13552
    • (2005) J Am Chem Soc , vol.127 , pp. 13548-13552
    • Jovanovic, T.1    Farid, R.2    Friesner, R.A.3    McDermott, A.E.4
  • 31
    • 0034962557 scopus 로고    scopus 로고
    • Pharmacophore and three-dimensional quantitative structure activity relationship methods for modeling cytochrome P450 active sites
    • Ekins S., de Groot M.J., and Jones J.P. Pharmacophore and three-dimensional quantitative structure activity relationship methods for modeling cytochrome P450 active sites. Drug Metab Dispos 29 (2001) 936-941
    • (2001) Drug Metab Dispos , vol.29 , pp. 936-941
    • Ekins, S.1    de Groot, M.J.2    Jones, J.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.