Structure of Human Cytidine Deaminase Bound to a Potent Inhibitor

Overview

Journal J Med Chem

Publisher American Chemical Society

Specialty Chemistry

Date 2005 Feb 4

PMID 15689149

Citations 34

Authors

Sang J Chung

J Christopher Fromme

Gregory L Verdine

Affiliations

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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.

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