Structural model of the Plasmodium falciparum thioredoxin reductase:a novel target for antimalarial drugs.

BACKGROUND Malaria, a scourge of mankind, imposes a huge socioeconomic burden in tropical countries. Emergence of multi-drug resistant malarial parasites impels us to explore novel drug targets. Thioredoxin reductase is a promising antimalarial drug target. METHODS The Thioredoxin reductase enzyme of Plasmodium falciparum was characterized in silico and protein disorder was predicted using available online tools. Since the crystal structure of Thioredoxin reductase of P. falciparum is not yet available, its three-dimensional structure was constructed by homology modeling using the high-resolution Thioredoxin reductase type 2 of mouse as a template. Obtained model was further refined by Molecular Dynamics (MD). RESULTS The model was stable during the simulation with the equilibrium root mean square deviation (RMSD) value of 1.2 A. Stereochemical evaluation revealed that 99.1% residues of the constructed model lie in the most favoured and allowed regions, thus, indicating a good quality model. CONCLUSION Results of this study will provide an insight into the structure of the Thioredoxin reductase of malarial parasite and aid in rational drug designing.