Structural bioinformatics study of PNP from Listeria monocytogenes

Protein Pept Lett. 2008;15(8):843-9. doi: 10.2174/092986608785203728.

Abstract

This work describes for the first time a model of Purine Nucleoside Phosphorylase from Listeria monocytogenes (LmPNP). We modeled the complexes of LmPNP with ligands in order to determine the structural basis for specificity. Comparative analysis of the model of LmPNP allowed identification of structural features responsible for ligand affinities.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Anti-Bacterial Agents / pharmacology
  • Anti-Bacterial Agents / therapeutic use
  • Apoenzymes / antagonists & inhibitors
  • Apoenzymes / chemistry
  • Apoenzymes / metabolism
  • Binding Sites
  • Computational Biology*
  • Drug Design
  • Humans
  • Ligands
  • Listeria monocytogenes / drug effects
  • Listeria monocytogenes / enzymology*
  • Listeriosis / drug therapy
  • Models, Molecular
  • Protein Structure, Tertiary
  • Purine-Nucleoside Phosphorylase / antagonists & inhibitors
  • Purine-Nucleoside Phosphorylase / chemistry*
  • Purine-Nucleoside Phosphorylase / metabolism
  • Substrate Specificity

Substances

  • Anti-Bacterial Agents
  • Apoenzymes
  • Ligands
  • Purine-Nucleoside Phosphorylase