Molecular modeling of the Plasmodium falciparum pre-mRNA splicing and nuclear export factor PfU52
- Subject Areas
- Biochemistry, Bioinformatics, Molecular Biology, Parasitology, Infectious Diseases
- RNA helicases, Homology modeling, Plasmodium falciparum, Structure-based drug design
- © 2013 Newo Soufo
- This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
- Cite this article
- 2013. Molecular modeling of the Plasmodium falciparum pre-mRNA splicing and nuclear export factor PfU52. PeerJ PrePrints 1:e106v1 https://doi.org/10.7287/peerj.preprints.106v1
UAP56/SUB2 is a DExD/H-box RNA helicase that is critically involved in pre-mRNA 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 structure-based, de novo design of new lead compounds. Here, we used homology modeling to construct a three-dimensional structure of PfU52 (PMDB ID: PM0079288), the Plasmodium falciparum ortholog of UAP56/SUB2. 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 design.
This abstract is a part of a submission under review with PeerJ.