Structure of human cytidine deaminase bound to a potent inhibitor.

Article Details

Citation

Chung SJ, Fromme JC, Verdine GL

Structure of human cytidine deaminase bound to a potent inhibitor.

J Med Chem. 2005 Feb 10;48(3):658-60.

PubMed ID
15689149 [ View in PubMed
]
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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Cytidine deaminaseP32320Details