Structural basis for androgen specificity and oestrogen synthesis in human aromatase

Thompson, E. A. & Siiteri, P. K. Utilization of oxygen and reduced nicotinamide adenine dinucleotide phosphate by human placental microsomes during aromatization of androstenedione. J. Biol. Chem. 249, 5364–5372 (1974)

Simpson, E. R. et al. Aromatase cytochrome P450, the enzyme responsible for estrogen biosynthesis. Endocr. Rev. 15, 342–355 (1994)

O’Neal Johnston, J. Aromatase inhibitors. Crit. Rev. Biochem. Mol. Biol. 33, 375–405 (1998)

Eisen, A., Trudeau, M., Shelley, W., Messersmith, H. & Pritchard, K. I. Aromatase inhibitors in adjuvant therapy for hormone receptor positive breast cancer: A systematic review. Cancer Treat. Rev. 34, 157–174 (2008)

Akhtar, M., Calder, D. L., Corina, D. L. & Wright, J. N. Mechanistic studies on C19-demethylation in oestrogen biosynthesis. Biochem. J. 201, 569–580 (1982)

Akhtar, M., Njar, V. C. & Wright, J. N. Mechanistic studies on aromatase and related C–C bond cleaving P-450 enzymes. J. Steroid Biochem. Mol. Biol. 44, 375–387 (1993)

Nakajin, S., Shinoda, M. & Hall, P. F. Purification to homogeneity of aromatase from human placenta. Biochem. Biophys. Res. Commun. 134, 704–710 (1986)

Kellis, J. T. & Vickery, L. E. Purification and characterization of human placental aromatase cytochrome P-450. J. Biol. Chem. 262, 4413–4420 (1987)

Zhou, D., Pompon, D. & Chen, S. Structure–function studies of human aromatase by site-directed mutagenesis: kinetic properties of mutants Pro-308–Phe, Tyr-361–Phe, Tyr-361–Leu, and Phe-406–Arg. Proc. Natl Acad. Sci. USA 88, 410–414 (1991)

Kadohama, N., Yarborough, C., Zhou, D., Chen, S. & Osawa, Y. Kinetic properties of aromatase mutants Pro 308Phe, Asp 309Asn, and Asp 309Ala and their interactions with aromatase inhibitors. J. Steroid Biochem. Mol. Biol. 43, 693–701 (1992)

Chen, S. et al. Structure–function studies of human aromatase. J. Steroid Biochem. Mol. Biol. 44, 347–356 (1993)

Laughton, C. A., Zvelebil, M. J. & Neidle, S. A detailed molecular model for human aromatase. J. Steroid Biochem. Mol. Biol. 44, 399–407 (1993)

Oh, S. S. & Robinson, C. H. Mechanism of human placental aromatase: a new active site model. J. Steroid Biochem. Mol. Biol. 44, 389–397 (1993)

Amarneh, B. & Simpson, E. R. Expression of a recombinant derivative of human aromatase P450 in insect cells utilizing the baculovirus vector system. Mol. Cell. Endocrinol. 109, R1–R5 (1995)

Graham-Lorence, S., Amarneh, B., White, R. E., Peterson, J. A. & Simpson, E. R. A three-dimensional model of aromatase cytochrome P450. Protein Sci. 4, 1065–1080 (1995)

Kao, Y. C., Korzekwa, K. R., Laughton, C. A. & Chen, S. Evaluation of the mechanism of aromatase cytochrome P450. A site-directed mutagenesis study. Eur. J. Biochem. 268, 243–251 (2001)

Chen, S. et al. Structure–function studies of aromatase and its inhibitors: a progress report. J. Steroid Biochem. Mol. Biol. 86, 231–237 (2003)

Hong, Y., Cho, M., Yuan, Y. C. & Chen, S. Molecular basis for the interaction of four different classes of substrates and inhibitors with human aromatase. Biochem. Pharmacol. 75, 1161–1169 (2008)

Lala, P. et al. Suppression of human cytochrome P450 aromatase activity by monoclonal and recombinant antibody fragments and identification of their stable antigenic complex. J. Steroid Biochem. Mol. Biol. 88, 235–245 (2004)

Nagano, S. & Poulos, T. L. Crystallographic study on the dioxygen complex of wild-type and mutant cytochrome P450cam. Implications for the dioxygen activation mechanism. J. Biol. Chem. 280, 31659–31663 (2005)

Nagano, S., Cupp-Vickery, J. R. & Poulos, T. L. Crystal structures of the ferrous dioxygen complex of wild-type cytochrome P450eryF and its mutants, A245S and A245T: investigation of the proton transfer system in P450eryF. J. Biol. Chem. 280, 22102–22107 (2005)

Williams, P. A. et al. Crystal structures of human cytochrome P450 3A4 bound to metyrapone and progesterone. Science 305, 683–686 (2004)

Rowland, P. et al. Crystal structure of human cytochrome P450 2D6. J. Biol. Chem. 281, 7614–7622 (2006)

Sansen, S., Hsu, M. H., Stout, C. D. & Johnson, E. F. Structural insight into the altered substrate specificity of human cytochrome P450 2A6 mutants. Arch. Biochem. Biophys. 464, 197–206 (2007)

Guallar, V., Baik, M. H., Lippard, S. J. & Friesner, R. A. Peripheral heme substituents control the hydrogen-atom abstraction chemistry in cytochromes P450. Proc. Natl Acad. Sci. USA 100, 6998–7002 (2003)

Podust, L. M., Poulos, T. L. & Waterman, M. R. Crystal structure of cytochrome P450 14α-sterol demethylase (CYP51) from Mycobacterium tuberculosis in complex with azole inhibitors. Proc. Natl Acad. Sci. USA 98, 3068–3073 (2001)

Hackett, J. C., Brueggemeier, R. W. & Hadad, C. M. The final catalytic step of cytochrome p450 aromatase: a density functional theory study. J. Am. Chem. Soc. 127, 5224–5237 (2005)

Pettersen, E. F. et al. UCSF Chimera—a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605–1612 (2004)

Cojocaru, V., Winn, P. J. & Wade, R. C. The ins and outs of cytochrome P450s. Biochim. Biophys. Acta 1770, 390–401 (2007)

Shimozawa, O. et al. Core glycosylation of cytochrome P-450(arom). Evidence for localization of N terminus of microsomal cytochrome P-450 in the lumen. J. Biol. Chem. 268, 21399–21402 (1993)

Yoshida, N. & Osawa, Y. Purification of human placental aromatase cytochrome P-450 with monoclonal antibody and its characterization. Biochemistry 30, 3003–3010 (1991)

Sato, R. & Omura, T. Cytochrome P-450 (Kodansha/Academic, 1978)

Otninowski, Z. & Minor, W. HKL Manual (Yale University, 1995)

Collaborative Computational Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760–763 (1994)

Emsley, P. & Cowtan, K. Coot: model building tools for molecular graphics. Acta Crystallogr. D 60, 2126–2132 (2004)

Murshudov, G. N., Vagin, A. A. & Dodson, E. J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53, 240–255 (1997)