期刊
JOURNAL OF MEDICINAL CHEMISTRY
卷 51, 期 15, 页码 4844-4848出版社
AMER CHEMICAL SOC
DOI: 10.1021/jm8003575
关键词
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The crystal structure of human 20 alpha-hydroxysteroid dehydrogenase (AKR1C1) in ternary complex with the coenzyme NADP(+) and the potent inhibitor 3,5-dichlorosalicylic acid was determined at a resolution of 1.8 angstrom. The inhibitor is held in place by a network of hydrogen bonding interactions with the active site residues Tyr55, His117, and His222. The important role of the nonconserved residues Leu54, His222, Leu306, and Leu308 in inhibitor binding and selectivity was determined by site-directed mutagenesis.
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