Journal
JOURNAL OF MEDICINAL CHEMISTRY
Volume 48, Issue 3, Pages 658-660Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jm0496279
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Funding
- NIGMS NIH HHS [R01 GM044853] Funding Source: Medline
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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.
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