Sang J. Chung, J. Christopher Fromme, G. Verdine
Jan 7, 2005
Citations
3
Influential Citations
72
Citations
Quality indicators
Journal
Journal of medicinal chemistry
Abstract
Human cytidine deaminase (CDA) is an enzyme prominent for its role in catalyzing metabolic processing of nucleoside-type anticancer and antiviral agents. It is thus a promising target for the development of small molecule therapeutic adjuvants. We report the first crystal structure of human CDA as a complex with a tight-binding inhibitor, diazepinone riboside 1. The structure reveals that inhibitor 1 is able to establish a canonical pi/pi-interaction with a key active site residue, Phe 137.