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Structure of Human Cytidine Deaminase Bound to a Potent Inhibitor

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journal contribution
posted on 10.02.2005, 00:00 by Sang 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.

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