Crystal Structure of Porcine Aldehyde Reductase at 2.0 A Resolution: Modeling an Inhibitor in the Active Site of the Enzyme

Autor: Ossama El-Kabbani, Deborah A. Carper, Michelle H. McGowan, Stephan L. Ginell
Rok vydání: 1996
Předmět:
Zdroj: Protein & Peptide Letters. 3:427-434
ISSN: 0929-8665
Popis: Abstract: Aldehyde reductase is an enzyme capable of metabolizing a wide variety of aldehydes to their corresponding alcohols.The X-ray crystal structure of porcine aldehyde reductase holoenzyme has been refined to a crystallographic R-factor of 0.20 at 2.0 A resolution. We have modeled the inhibitor zopolrestat in the active site of porcine aldehyde reductase in order to obtain a picture of the binding conformation of inhibitors to the enzyme.
Databáze: OpenAIRE