Molecular modeling, structural analysis and identification of ligand binding sites of trypanothione reductase from Leishmania mexicana


Mutlu O.

JOURNAL OF VECTOR BORNE DISEASES, vol.50, no.1, pp.38-44, 2013 (Journal Indexed in SCI) identifier

  • Publication Type: Article / Article
  • Volume: 50 Issue: 1
  • Publication Date: 2013
  • Title of Journal : JOURNAL OF VECTOR BORNE DISEASES
  • Page Numbers: pp.38-44

Abstract

Background & objectives: Trypanothione reductase (TR) is a member of FAD-dependent NADPH oxidoreductase protein family and it is a key enzyme which connects the NADPH and the thiol-based redox system. Inhibition studies indicate that TR is an essential enzyme for parasite survival. Therefore, it is an attractive target enzyme for novel drug candidates. There is no structural model for TR of Leishmania mexicana (LmTR) in the protein databases. In this work, 3D structure of TR from L. mexicana was identified by template-based in silico homology modeling method, resultant model was validated, structurally analyzed and possible ligand binding pockets were identified.