Active site analysis of 17β-hydroxysteroid dehydrogenase type 1 enzyme complexes with SPROUT

Abstract Estrogens, especially estradiol, have been shown to stimulate the proliferation of hormone-dependent types of breast cancer cells. 17β-Hydroxysteroid dehydrogenase type 1 (17β-HSD1) enzyme catalyses the synthesis of the active female estrogen, estradiol and is thus an attractive target for structure-based ligand design for the prevention and control of breast tumour growth. In this study, the active site of 17β-HSD1 has been reviewed, and three crystal structure complexes (estradiol/NADP + , equilin/NADP + , dehydroepiandrosterone) of 17β-HSD1 have been selected to be analysed for de novo ligand design. The boundary surface, hydrophobic interactions and hydrogen bonding sites in the ligand binding domain for each ligand complex were analysed to create a comprehensive image of the active site.