Research Article
Structure Analysis of Interacting Domains of RNA Dependent RNA Polymerase (Rdrp) Complex in Nipah Virus
| Md. Jahangir Alam1, Mst. Saleha Sultana1, Jahed Ahmed1*, Auditi Purkaystha1, Abdullah Zubaer2, Mohammad Lashkar2, Kaniz Fatema1 and Md. Rabiul Awal1 | |
| 1Department of Genetic Engineering and Biotechnology, Shahjalal University of Science and Technology, Sylhet-3114, Bangladesh | |
| 2Swapnojaatra Bioresearch Laboratory, Dhaka-1215, Bangladesh | |
| Corresponding Author : | Jahed Ahmed Department of Genetic Engineering and Biotechnology Shahjalal University of Science and Technology Sylhet-3114, Bangladesh Tel: +8801726251159 Fax: +880821-715257 E-mail: jahedahmed@student.sust.edu |
| Received: October 01, 2015; Accepted: October 30, 2015; Published: November 06, 2015 | |
| Citation: Alam MJ, Sultana MS, Ahmed J, Purkaystha A, Zubaer A, et al. (2015) Structure Analysis of Interacting Domains of RNA Dependent RNA Polymerase (Rdrp) Complex in Nipah Virus. Biochem Physiol 4:187. doi:10.4172/2168-9652.1000187 | |
| Copyright: © 2015 Alam MJ, et al. 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. | |
Abstract
Nipah virus is an emerging zoonotic paramyxovirus that is responsible for severe outbreaks in humans and livestocks. This negative stranded RNA virus carries RNA-dependent RNA polymerase (RdRp) complex which is required for viral RNA replication and transcription as a catalytic subunit of viral replicase. We have investigated the 3D structures of four domains from three proteins- Nucleocapsid (N), Phosphoprotein (P) and Polymerase (L) which contribute to form RdRp complex. The presence of intrinsic disorder regions in those proteins under native condition which made the in vitro study of structure difficult. In our study, the 3D homology models of the domain Alpha MoRE and PXD (forming N-P complex), and domain PMD and Domain I (forming P-L complex) were generated and evaluated. Protein-protein docking studies of these four domains was performed which elucidated the structural aspects of RdRp complex and also showed the nature of individual interaction (N-P and P-L). The evidence of the weak binding of Alpha MoRE with PXD than the binding affinity of PMD to Domain I have suggested that, the Alpha MoRE-PXD interaction as a valuable drug target.
