Structural highlights
Function
[CDD_HUMAN] This enzyme scavenge exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of human cytidine deaminase bound to a potent inhibitor.,Chung SJ, Fromme JC, Verdine GL J Med Chem. 2005 Feb 10;48(3):658-60. PMID:15689149[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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. PMID:15689149 doi:10.1021/jm0496279
