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

Mutlu O.

JOURNAL OF VECTOR BORNE DISEASES, cilt.50, sa.1, ss.38-44, 2013 (SCI-Expanded) identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 50 Sayı: 1
  • Basım Tarihi: 2013
  • Dergi Adı: JOURNAL OF VECTOR BORNE DISEASES
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.38-44
  • Marmara Üniversitesi Adresli: Evet

Özet

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.