posted on 2005-02-10, 00:00authored bySang J. Chung, J. Christopher Fromme, Gregory L. Verdine
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 π/π-interaction with a key active
site residue, Phe 137.