1AFS

RECOMBINANT RAT LIVER 3-ALPHA-HYDROXYSTEROID DEHYDROGENASE (3-ALPHA-HSD) COMPLEXED WITH NADP AND TESTOSTERONE

Summary for 1AFS

• Entry DOI: 10.2210/pdb1afs/pdb
• Descriptor: 3-ALPHA-HYDROXYSTEROID DEHYDROGENASE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, TESTOSTERONE, ... (4 entities in total)
• Functional Keywords: oxidoreductase, nad
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cytoplasm: P23457
• Total number of polymer chains: 2
• Total formula weight: 76448.95

Authors

Bennett, M.J.,Albert, R.H.,Jez, J.M.,Ma, H.,Penning, T.M.,Lewis, M. (deposition date: 1997-03-13, release date: 1997-10-08, Last modification date: 2024-05-22)

Primary citation

Bennett, M.J.,Albert, R.H.,Jez, J.M.,Ma, H.,Penning, T.M.,Lewis, M.
Steroid recognition and regulation of hormone action: crystal structure of testosterone and NADP+ bound to 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase.
Structure, 5:799-812, 1997

PubMed Abstract: Mammalian 3 alpha-hydroxysteroid dehydrogenases (3 alpha-HSDs) modulate the activities of steroid hormones by reversibly reducing their C3 ketone groups. In steroid target tissues, 3 alpha-HSDs act on 5 alpha-dihydrotestosterone, a potent male sex hormone (androgen) implicated in benign prostate hyperplasia and prostate cancer. Rat liver 3 alpha-HSD belongs to the aldo-keto reductase (AKR) superfamily and provides a model for mammalian 3 alpha-, 17 beta- and 20 alpha-HSDs, which share > 65% sequence identity. The determination of the structure of 3 alpha-HSD in complex with NADP+ and testosterone (a competitive inhibitor) will help to further our understanding of steroid recognition and hormone regulation by mammalian HSDs.

PubMed: 9261071
DOI: 10.1016/S0969-2126(97)00234-7

Experimental method

X-RAY DIFFRACTION (2.5 Å)