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Structure-based drug design using the crystal structure of human 17beta-hydroxysteroid dehydrogenase type 1 (17beta-HSD1) led to the discovery of novel, selective, and the most potent inhibitors of 17beta-HSD1 reported to date. Compounds 1 and 2 contain a side chain with an m-pyridylmethyl-amide functionality extended from the 16beta position of a steroid scaffold. A mode of binding is proposed for these inhibitors, and 2 is a steroid-based 17beta-HSD1 inhibitor with the potential for further development.

Original publication

DOI

10.1021/jm049045r

Type

Journal article

Journal

J Med Chem

Publication Date

21/04/2005

Volume

48

Pages

2759 - 2762

Keywords

17-Hydroxysteroid Dehydrogenases, Antineoplastic Agents, Cell Line, Tumor, Crystallography, X-Ray, Estrone, Humans, Models, Molecular, Molecular Structure, Pyridines, Stereoisomerism, Structure-Activity Relationship