Structure of human cytidine deaminase bound to a potent inhibitor

J Med Chem. 2005 Feb 10;48(3):658-60. doi: 10.1021/jm0496279.

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.

MeSH terms

  • Azepines / chemistry*
  • Binding Sites
  • Crystallography, X-Ray
  • Cytidine Deaminase / antagonists & inhibitors*
  • Cytidine Deaminase / chemistry*
  • Enzyme Inhibitors / chemistry*
  • Humans
  • Models, Molecular
  • Molecular Structure
  • Protein Conformation

Substances

  • Azepines
  • Enzyme Inhibitors
  • diazepinone riboside
  • Cytidine Deaminase

Associated data

  • PDB/1MQ0