Authors: Alain N S Newo
Publish Date: 2014/05/27
Volume: 33, Issue: 4, Pages: 354-368
Abstract
UAP56/SUB2 is a DExD/Hbox RNA helicase that is critically involved in premRNA splicing and mRNA nuclear export This helicase is broadly conserved and essential in many eukaryotic lineages including protozoan and metazoan parasites Previous research suggests that helicases from parasites could be promising drug targets for treating parasitic diseases Accordingly characterizing the structure and function of these proteins is of interest for structurebased de novo design of new lead compounds Here we used homology modeling to construct a threedimensional structure of PfU52 PMDB ID PM0079288 the Plasmodium falciparum ortholog of UAP56/SUB2 and explored the detailed architecture of its functional sites Comparative in silico analysis revealed that although PfU52 shared many physicochemical structural and dynamic similarities with its human homolog it also displayed some unique features that could be exploited for drug designWe are grateful to Dr Keely L Walker and her team City of Hope Beckman Research Institute for critically reading and editing the manuscript prior to submission We thank the California Institute of Technology Caltech Library staff for providing access to some of the scientific literature used in this study
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