Molecular Modeling of the Plasmodium falciparum Pre-mRNA Splicing and Nuclear Export Factor PfU52
| Autor: | Alain N. S. Newo |
|---|---|
| Rok vydání: | 2014 |
| Předmět: |
Models
Molecular In silico Molecular Sequence Data Plasmodium falciparum Protozoan Proteins Bioengineering Sequence alignment Biochemistry Analytical Chemistry DEAD-box RNA Helicases Computer Simulation Amino Acid Sequence Homology modeling Nuclear export signal Genetics Binding Sites biology Organic Chemistry Helicase Hydrogen-Ion Concentration biology.organism_classification RNA Helicase A RNA splicing biology.protein RNA Thermodynamics Sequence Alignment |
| Zdroj: | The Protein Journal. 33:354-368 |
| ISSN: | 1875-8355 1572-3887 |
| DOI: | 10.1007/s10930-014-9566-x |
| Popis: | 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, 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 design. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full text from SpringerLink