Structural characterization of pfSerine hydroxymethyltransferase: A novel target for malaria

摘要

New chemotherapeutic targets are urgently required to control malaria, a tropical disease caused by?Plasmodium?sp., which has been haunting mankind for ages. Serine hydroxymethyltransferase (SHMT) plays a major role in DNA biosynthesis.PfSHMT?sequence compared for identities with hu mtSHMT (2A7V), T.ThHb8SHMT (2DKJ) and Rabbit cytSHMT (1EQB). ClustralW and Modeller9v3 were used for multiple sequence alignment and homology modeling of?PfSHMTrespectively. Validation of the stereochemical quality and structure analysis for the developed?PfSHMT?model were done with PROCHECK and WHATIF programs. The Z-score as determined by ProSA web analysis. The catalytic residues were Aspartic acid-208, histidine-129, 132, 211, lysine-237, threonine-234, which were conserved in the developed model of SHMT of?Plasmodium falciparum. The developed?PfSHMT?model submitted to PMDB has been accepted with less than 3% stereochemical check failures. The present study would provide valuable information for search and rational drug design of new generation of wide spectrum?of novel antimalarial?drugs.