Crystal structure of calf spleen purine nucleoside phosphorylase complexed to a novel purine analogue

FEBS Lett. 2007 Oct 30;581(26):5082-6. doi: 10.1016/j.febslet.2007.09.051. Epub 2007 Oct 2.

Abstract

The combined use of a rapid virtual screen of a small fragment library together with a single point enzyme assay has been used for the discovery of novel PNP inhibitors. The availability of readily soakable crystals of bovine PNP has allowed the approach to be experimentally validated by determining the crystal structure of one of the inhibitor-PNP complexes. Comparison of the experimentally determined binding mode with that predicted by the virtual screening shows them to be similar. This represents a starting point for the growth of the ligand into a higher affinity inhibitor.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cattle
  • Crystallography, X-Ray
  • Drug Evaluation, Preclinical
  • Enzyme Inhibitors / chemistry*
  • Enzyme Inhibitors / pharmacology
  • Protein Conformation
  • Purine-Nucleoside Phosphorylase / antagonists & inhibitors*
  • Purine-Nucleoside Phosphorylase / chemistry*
  • Purines / chemistry*
  • Purines / pharmacology
  • Spleen / enzymology*

Substances

  • Enzyme Inhibitors
  • Purines
  • Purine-Nucleoside Phosphorylase