A 3D Model of CYP1B1 Explains the Dominant 4-Hydroxylation of Estradiol
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- Toshimasa Itoh
- Laboratory of Drug Design and Medicinal Chemistry, Showa Pharmaceutical University, 3-3165 Higashi-Tamagawagakuen, Machida, Tokyo 194-8543, Japan, Faculty of Human Health Sciences, Matsumoto University, 2095-1 Niimura, Matsumoto 390-1295, Japan, and Institute for Environmental Sciences, University of Shizuoka, 52-1 Yada, Suruga, Shizuoka 422-8526, Japan
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- Hitomi Takemura
- Laboratory of Drug Design and Medicinal Chemistry, Showa Pharmaceutical University, 3-3165 Higashi-Tamagawagakuen, Machida, Tokyo 194-8543, Japan, Faculty of Human Health Sciences, Matsumoto University, 2095-1 Niimura, Matsumoto 390-1295, Japan, and Institute for Environmental Sciences, University of Shizuoka, 52-1 Yada, Suruga, Shizuoka 422-8526, Japan
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- Kayoko Shimoi
- Laboratory of Drug Design and Medicinal Chemistry, Showa Pharmaceutical University, 3-3165 Higashi-Tamagawagakuen, Machida, Tokyo 194-8543, Japan, Faculty of Human Health Sciences, Matsumoto University, 2095-1 Niimura, Matsumoto 390-1295, Japan, and Institute for Environmental Sciences, University of Shizuoka, 52-1 Yada, Suruga, Shizuoka 422-8526, Japan
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- Keiko Yamamoto
- Laboratory of Drug Design and Medicinal Chemistry, Showa Pharmaceutical University, 3-3165 Higashi-Tamagawagakuen, Machida, Tokyo 194-8543, Japan, Faculty of Human Health Sciences, Matsumoto University, 2095-1 Niimura, Matsumoto 390-1295, Japan, and Institute for Environmental Sciences, University of Shizuoka, 52-1 Yada, Suruga, Shizuoka 422-8526, Japan
書誌事項
- 公開日
- 2010-05-12
- 資源種別
- journal article
- DOI
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- 10.1021/ci1000554
- 公開者
- American Chemical Society (ACS)
この論文をさがす
説明
CYP1A1 and CYP1A2 exhibit catalytic activity predominantly for the 2-hydroxylation of estradiol, whereas CYP1B1 exhibits catalytic activity predominantly for 4-hydroxylation of estradiol. To understand why CYP1B1 predominantly hydroxylates the 4-position of estradiol, we constructed three-dimensional structures of CYP1A1 and CYP1B1 by homology modeling, using the crystal structure of CYP1A2, and studied the docking mode of estradiol with CYP1A1, CYP1A2, and CYP1B1. The results demonstrated that two particular amino acid residues for each CYP, namely Thr124 and Phe260 of CYP1A2, Ser122 and Phe258 of CYP1A1, and Ala133 and Asn265 of CYP1B1, play an important role in estradiol recognition.
収録刊行物
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- Journal of Chemical Information and Modeling
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Journal of Chemical Information and Modeling 50 (6), 1173-1178, 2010-05-12
American Chemical Society (ACS)
