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• W2029656887 abstract "A three-dimensional (3-D) structure of human aromatase (CYP 19) was modeled on the basis of the crystal structure of rabbit CYP2C5, the first solved X-ray structure of an eukaryotic cytochrome P450 and was evaluated by docking S-fadrozole and the steroidal competitive inhibitor (19R)-10-thiiranylestr-4-ene-3,17-dione, into the enzyme active site. According to a previous pharmacophoric hypothesis described in the literature, the cyano group of S-fadrozole partially mimics the steroid backbone C(17) carbonyl group of (19R)-10-thiiranylestr-4-ene-3,17-dione, and was oriented in a favorable position for H-bonding with the newly identified positively charged residues Lys 119 and Arg435. In addition, this model is consistent with the recent combined mutagenesis/modeling studies already published concerning the roles ofAsp309 and His480 in the aromatization of the steroid A ring." @default.
• W2029656887 created "2016-06-24" @default.
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• W2029656887 date "2005-01-01" @default.
• W2029656887 modified "2023-10-18" @default.
• W2029656887 title "Three-dimensional model of cytochrome P450 human aromatase" @default.
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• W2029656887 doi "https://doi.org/10.1080/14756360500220574" @default.
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