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Volumn 482, Issue 7383, 2012, Pages 116-119

Structures of cytochrome P450 17A1 with prostate cancer drugs abiraterone and TOK-001

Author keywords

[No Author keywords available]

Indexed keywords

ABIRATERONE; CYTOCHROME P450 17; GALETERONE; HEME; STEROID;

EID: 84856477784     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature10743     Document Type: Review
Times cited : (295)

References (43)
  • 1
    • 79951665862 scopus 로고    scopus 로고
    • The molecular biology, biochemistry, and physiology of human steroidogenesis and its disorders
    • Miller, W. L. & Auchus, R. J. The molecular biology, biochemistry, and physiology of human steroidogenesis and its disorders. Endocr. Rev. 32, 81-151 (2011).
    • (2011) Endocr. Rev. , vol.32 , pp. 81-151
    • Miller, W.L.1    Auchus, R.J.2
  • 2
    • 67449119425 scopus 로고    scopus 로고
    • Antitumor activity with CYP17 blockade indicates that castration-resistant prostate cancer frequently remains hormone driven
    • Attard, G., Reid, A. H., Olmos, D. & de Bono, J. S. Antitumor activity with CYP17 blockade indicates that castration-resistant prostate cancer frequently remains hormone driven. Cancer Res. 69, 4937-4940 (2009).
    • (2009) Cancer Res. , vol.69 , pp. 4937-4940
    • Attard, G.1    Reid, A.H.2    Olmos, D.3    De Bono, J.S.4
  • 3
    • 51449124047 scopus 로고    scopus 로고
    • Targeting CYP17: Established and novel approaches in prostate cancer
    • Yap, T. A., Carden, C. P., Attard, G. & de Bono, J. S. Targeting CYP17: Established and novel approaches in prostate cancer. Curr. Opin. Pharmacol. 8, 449-457 (2008).
    • (2008) Curr. Opin. Pharmacol. , vol.8 , pp. 449-457
    • Yap, T.A.1    Carden, C.P.2    Attard, G.3    De Bono, J.S.4
  • 5
    • 79957443342 scopus 로고    scopus 로고
    • Abiraterone and increased survival in metastatic prostate cancer
    • de Bono, J. S. et al. Abiraterone and increased survival in metastatic prostate cancer. N. Engl. J. Med. 364, 1995-2005 (2011).
    • (2011) N. Engl. J. Med. , vol.364 , pp. 1995-2005
    • De Bono, J.S.1
  • 6
    • 79851510026 scopus 로고    scopus 로고
    • Novel therapeutic strategies for castration resistant prostate cancer: Inhibition of persistent androgen production and androgen receptor mediated signaling
    • Molina, A. & Belidegrun, A. Novel therapeutic strategies for castration resistant prostate cancer: inhibition of persistent androgen production and androgen receptor mediated signaling. J. Urol. 185, 787-794 (2011).
    • (2011) J. Urol. , vol.185 , pp. 787-794
    • Molina, A.1    Belidegrun, A.2
  • 7
    • 0031965926 scopus 로고    scopus 로고
    • The regulation of human P450c17 activity: Relationship to premature adrenarche, insulin resistance and the polycystic ovary syndrome
    • DOI 10.1016/S1043-2760(98)00016-2, PII S1043276098000162
    • Auchus, R. J., Geller, D. H., Lee, T. C. & Miller, W. L. The regulation of human P450c17 activity: relationship to premature adrenarche, insulin resistance and the polycystic ovary syndrome. Trends Endocrinol. Metab. 9, 47-50 (1998). (Pubitemid 28207611)
    • (1998) Trends in Endocrinology and Metabolism , vol.9 , Issue.2 , pp. 47-50
    • Auchus, R.J.1    Geller, D.H.2    Lee, T.C.3    Miller, W.L.4
  • 8
    • 53749090666 scopus 로고    scopus 로고
    • Phase i clinical trial of a selective inhibitor of CYP17, abiraterone acetate, confirms that castration-resistant prostate cancer commonly remains hormone driven
    • Attard, G. et al. Phase I clinical trial of a selective inhibitor of CYP17, abiraterone acetate, confirms that castration-resistant prostate cancer commonly remains hormone driven. J. Clin. Oncol. 26, 4563-4571 (2008).
    • (2008) J. Clin. Oncol. , vol.26 , pp. 4563-4571
    • Attard, G.1
  • 9
    • 57849152888 scopus 로고    scopus 로고
    • The Coffey Lecture: Steroidogenic enzyme inhibitors and hormone dependent cancer
    • Brodie, A., Njar, V., Macedo, L. F., Vasitis, T. S. & Sabnis, G. The Coffey Lecture: steroidogenic enzyme inhibitors and hormone dependent cancer. Urol. Oncol. 27, 53-63 (2009).
    • (2009) Urol. Oncol. , vol.27 , pp. 53-63
    • Brodie, A.1    Njar, V.2    MacEdo, L.F.3    Vasitis, T.S.4    Sabnis, G.5
  • 10
    • 0027198401 scopus 로고
    • Expression and purification of functional human 17α-hydroxylase/17, 20- lyase (P450c17) in Escherichia coli. Use of this system for study of a novel form of combined 17α-hydroxylase/17,20-lyase deficiency
    • Imai, T. et al. Expression and purification of functional human 17a-hydroxylase/17, 20-lyase (P450c17) in Escherichia coli. Use of this system for study of a novel form of combined 17a-hydroxylase/17, 20-lyase deficiency. J. Biol. Chem. 268, 19681-19689 (1993). (Pubitemid 23270759)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.26 , pp. 19681-19689
    • Imai, T.1    Globerman, H.2    Gertner, J.M.3    Kagawa, N.4    Waterman, M.R.5
  • 11
    • 77951901129 scopus 로고    scopus 로고
    • Structural overview of the nuclear receptor superfamily: Insights into physiology and therapeutics
    • Huang, P., Chandra, V. & Rastinejad, F. Structural overview of the nuclear receptor superfamily: insights into physiology and therapeutics. Annu. Rev. Physiol. 72, 247-272 (2010).
    • (2010) Annu. Rev. Physiol. , vol.72 , pp. 247-272
    • Huang, P.1    Chandra, V.2    Rastinejad, F.3
  • 12
    • 33646138016 scopus 로고    scopus 로고
    • Comparison of crystal structures of human androgen receptor ligand-binding domain complexed with various agonists reveals molecular determinants responsible for binding affinity
    • Pereira de Jésus-Tran, K. et al. Comparison of crystal structures of human androgen receptor ligand-binding domain complexed with various agonists reveals molecular determinants responsible for binding affinity. Protein Sci. 15, 987-999 (2006).
    • (2006) Protein Sci. , vol.15 , pp. 987-999
    • Pereira De Jésus-Tran, K.1
  • 13
    • 53349101498 scopus 로고    scopus 로고
    • Androgen receptor inactivation contributes to antitumor efficacy of 17a-hydroxylase/17, 20-lyase inhibitor 3b-hydroxy-17-(1H-benzimidazole-1-yl) androsta-5, 16-diene in prostate cancer
    • Vasaitis, T. et al. Androgen receptor inactivation contributes to antitumor efficacy of 17a-hydroxylase/17, 20-lyase inhibitor 3b-hydroxy-17-(1H-benzimidazole-1-yl)androsta-5, 16-diene in prostate cancer. Mol. Cancer Ther. 7, 2348-2357 (2008).
    • (2008) Mol. Cancer Ther. , vol.7 , pp. 2348-2357
    • Vasaitis, T.1
  • 14
    • 58149339806 scopus 로고    scopus 로고
    • Structural basis for androgen specificity and oestrogen synthesis in human aromatase
    • Ghosh, D., Griswold, J., Erman, M. & Pangborn, W. Structural basis for androgen specificity and oestrogen synthesis in human aromatase. Nature 457, 219-223 (2009).
    • (2009) Nature , vol.457 , pp. 219-223
    • Ghosh, D.1    Griswold, J.2    Erman, M.3    Pangborn, W.4
  • 15
    • 79953148368 scopus 로고    scopus 로고
    • Structural basis for three-step sequential catalysis by the cholesterol side chain cleavage enzyme CYP11A1
    • Mast, N. et al. Structural basis for three-step sequential catalysis by the cholesterol side chain cleavage enzyme CYP11A1. J. Biol. Chem. 286, 5607-5613 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 5607-5613
    • Mast, N.1
  • 17
    • 68549132307 scopus 로고    scopus 로고
    • Steroid 17a-hydroxylase deficiency: Functional characterization of four mutations (A174E, V178D, R440C, L465P) in the CYP17A1 gene
    • Dhir, V. et al. Steroid 17a-hydroxylase deficiency: Functional characterization of four mutations (A174E, V178D, R440C, L465P) in the CYP17A1 gene. J. Clin. Endocrinol. Metab. 94, 3058-3064 (2009).
    • (2009) J. Clin. Endocrinol. Metab. , vol.94 , pp. 3058-3064
    • Dhir, V.1
  • 18
    • 77951284413 scopus 로고    scopus 로고
    • Clinical, genetic and functional characteristics of three novel CYP17A1 mutations causing combined 17a-hydroxylase/17, 20-lyase deficiency
    • Rosa, S. et al. Clinical, genetic and functional characteristics of three novel CYP17A1 mutations causing combined 17a-hydroxylase/17, 20-lyase deficiency. Horm. Res. Paediatr. 73, 198-204 (2010).
    • (2010) Horm. Res. Paediatr. , vol.73 , pp. 198-204
    • Rosa, S.1
  • 19
    • 74049113684 scopus 로고    scopus 로고
    • Novel CYP17A1 mutation in a Japanese patient with combined 17a-hydroxylase/17, 20-lyase deficiency
    • Katsumata, N., Ogawa, E., Fujiwara, I. & Fujikura, K. Novel CYP17A1 mutation in a Japanese patient with combined 17a-hydroxylase/17, 20-lyase deficiency. Metabolism 59, 275-278 (2010).
    • (2010) Metabolism , vol.59 , pp. 275-278
    • Katsumata, N.1    Ogawa, E.2    Fujiwara, I.3    Fujikura, K.4
  • 21
    • 68549085136 scopus 로고    scopus 로고
    • Novel P450c17 mutation H373D causing combined 17a-hydroxylase/17, 20-lyase deficiency
    • Sahakitrungruang, T., Tee, M. K., Speiser, P. W. & Miller, W. L. Novel P450c17 mutation H373D causing combined 17a-hydroxylase/17, 20-lyase deficiency. J. Clin. Endocrinol. Metab. 94, 3089-3092 (2009).
    • (2009) J. Clin. Endocrinol. Metab. , vol.94 , pp. 3089-3092
    • Sahakitrungruang, T.1    Tee, M.K.2    Speiser, P.W.3    Miller, W.L.4
  • 24
    • 0034840366 scopus 로고    scopus 로고
    • Pitfalls in characterizing P450c17 mutations associated with isolated 17,20-lyase deficiency
    • DOI 10.1210/jc.86.9.4416
    • Gupta, M. K., Geller, D. H. & Auchus, R. J. Pitfalls in characterizing P450c17 mutations associated with isolated 17, 20-lyase deficiency. J. Clin. Endocrinol. Metab. 86, 4416-4423 (2001). (Pubitemid 32848568)
    • (2001) Journal of Clinical Endocrinology and Metabolism , vol.86 , Issue.9 , pp. 4416-4423
    • Gupta, M.K.1    Geller, D.H.2    Auchus, R.J.3
  • 26
    • 0032488666 scopus 로고    scopus 로고
    • 5 augments the 17,20-lyase activity of human P450c17 without direct electron transfer
    • DOI 10.1074/jbc.273.6.3158
    • Auchus, R. J., Lee, T. C. & Miller, W. L. Cytochrome b5 augments the 17, 20-lyase activity of human P450c17 without direct electron transfer. J. Biol. Chem. 273, 3158-3165 (1998). (Pubitemid 28109723)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.6 , pp. 3158-3165
    • Auchus, R.J.1    Lee, T.C.2    Miller, W.L.3
  • 27
    • 77950244867 scopus 로고    scopus 로고
    • A single amino acid residue Ala 105, confers 16a-hydroxylase activity to human cytochrome P450 17a-hydroxylase/17, 20 lyase
    • Swart, A. C., Storbeck, K. H. & Swart, P. A single amino acid residue, Ala 105, confers 16a-hydroxylase activity to human cytochrome P450 17a-hydroxylase/17, 20 lyase. J. Steroid Biochem. Mol. Biol. 119, 112-120 (2010).
    • (2010) J. Steroid Biochem. Mol. Biol. , vol.119 , pp. 112-120
    • Swart, A.C.1    Storbeck, K.H.2    Swart, P.3
  • 28
    • 77954621604 scopus 로고    scopus 로고
    • Molecular modeling on inhibitor complexes and active-site dynamics of cytochrome P450 C17, a target for prostate cancer therapy
    • Haider, S. M., Patel, J. S., Poojari, C. S. & Neidle, S. Molecular modeling on inhibitor complexes and active-site dynamics of cytochrome P450 C17, a target for prostate cancer therapy. J. Mol. Biol. 400, 1078-1098 (2010).
    • (2010) J. Mol. Biol. , vol.400 , pp. 1078-1098
    • Haider, S.M.1    Patel, J.S.2    Poojari, C.S.3    Neidle, S.4
  • 30
    • 49149103977 scopus 로고    scopus 로고
    • Engineering expression and purification of "soluble" human cytochrome P45017a and its functional characterization
    • Pechurskaya, T. A., Lukashevich, O. P., Gilep, A. A. & Usanov, S. A. Engineering, expression, and purification of "soluble" human cytochrome P45017a and its functional characterization. Biochemistry 73, 806-811 (2008).
    • (2008) Biochemistry , vol.73 , pp. 806-811
    • Pechurskaya, T.A.1    Lukashevich, O.P.2    Gilep, A.A.3    Usanov, S.A.4
  • 32
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 37
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291 (1993).
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 38
    • 66649122018 scopus 로고    scopus 로고
    • Key residues controlling binding of diverse ligands to human cytochrome P450 2A enzymes
    • DeVore, N. M. et al. Key residues controlling binding of diverse ligands to human cytochrome P450 2A enzymes. Drug Metab. Dispos. 37, 1319-1327 (2009).
    • (2009) Drug Metab. Dispos. , vol.37 , pp. 1319-1327
    • Devore, N.M.1
  • 41
    • 0037434582 scopus 로고    scopus 로고
    • Surflex: Fully automatic flexible molecular docking using a molecular similarity-based search engine
    • DOI 10.1021/jm020406h
    • Jain, A. N. Surflex: fully automatic flexible molecular docking using a molecular similarity-based search engine. J. Med. Chem. 46, 499-511 (2003). (Pubitemid 36182752)
    • (2003) Journal of Medicinal Chemistry , vol.46 , Issue.4 , pp. 499-511
    • Jain, A.N.1
  • 42
    • 1242352932 scopus 로고    scopus 로고
    • Synthesis of hydroxy derivatives of highly potent non-steroidal CYP 17 inhibitors as potential metabolites and evaluation of their activity by a non cellular assay using recombinant human enzyme
    • DOI 10.1080/14756360310001640913
    • Hutschenreuter, T. U., Ehmer, P. B. & Hartmann, R. W. Synthesis of hydroxy derivatives of highly potent non-steroidal CYP 17 inhibitors as potential metabolites and evaluation of their activity by a non cellular assay using recombinant human enzyme. J. Enzyme Inhib. Med. Chem. 19, 17-32 (2004). (Pubitemid 38239927)
    • (2004) Journal of Enzyme Inhibition and Medicinal Chemistry , vol.19 , Issue.1 , pp. 17-32
    • Hutschenreuter, T.U.1    Ehmer, P.B.2    Hartmann, R.W.3
  • 43
    • 0024518203 scopus 로고
    • Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed mutagenesis
    • Shen, A. L., Porter, T. D., Wilson, T. E. & Kasper, C. B. Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed mutagenesis. J. Biol. Chem. 264, 7584-7589 (1989). (Pubitemid 19119176)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.13 , pp. 7584-7589
    • Shen, A.L.1    Porter, T.D.2    Wilson, T.E.3    Kasper, C.B.4


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