Use of Geometrical Docking Algorithm to Explore Species Specific Differences in Proyl-tRNA Synthetases

Abstract

Prolyl-tRNA synthetases belong to a class of enzymes that play a pivotal role in the protein synthesis. These enzymes are responsible for attaching the amino acid, proline, to the 3’ end of the prolyl-tRNA. The structures and domain architectures of these enzymes differ considerably between human and their pathogenic analogs. Identifying the differences of recognition elements present in the two active sites can lead to selective inhibitors based on structure. In the present study, computer-aided docking and simulations have been carried out on several substrate (proline) and inhibitor (halofuginone) analogs.