Comparison of crystal structures of human type 3 3alpha-hydroxysteroid dehydrogenase reveals an "induced-fit" mechanism and a conserved basic motif involved in the binding of androgen.

@article{Couture2005ComparisonOC,
  title={Comparison of crystal structures of human type 3 3alpha-hydroxysteroid dehydrogenase reveals an "induced-fit" mechanism and a conserved basic motif involved in the binding of androgen.},
  author={Jean-François Couture and Karine Pereira de J{\'e}sus-Tran and A Roy and Line Cantin and P Cote and Pierre Legrand and Van Luu-The and Fernand Labrie and Rock Breton},
  journal={Protein science : a publication of the Protein Society},
  year={2005},
  volume={14 6},
  pages={1485-97}
}
The aldo-keto reductase (AKR) human type 3 3alpha-hydroxysteroid dehydrogenase (h3alpha-HSD3, AKR1C2) plays a crucial role in the regulation of the intracellular concentrations of testosterone and 5alpha-dihydrotestosterone (5alpha-DHT), two steroids directly linked to the etiology and the progression of many prostate diseases and cancer. This enzyme also binds many structurally different molecules such as 4-hydroxynonenal, polycyclic aromatic hydrocarbons, and indanone. To understand the… CONTINUE READING