Structure Analysis of Interacting Domains of RNA Dependent RNA Polymerase (Rdrp) Complex in Nipah Virus | OMICS International | Abstract
ISSN: 2168-9652

Biochemistry & Physiology: Open Access
Open Access

Our Group organises 3000+ Global Conferenceseries Events every year across USA, Europe & Asia with support from 1000 more scientific Societies and Publishes 700+ Open Access Journals which contains over 50000 eminent personalities, reputed scientists as editorial board members.

Open Access Journals gaining more Readers and Citations
700 Journals and 15,000,000 Readers Each Journal is getting 25,000+ Readers

This Readership is 10 times more when compared to other Subscription Journals (Source: Google Analytics)

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: [email protected]
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.


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.


Recommended Conferences
Indexed In
  • CAS Source Index (CASSI)
  • Index Copernicus
  • Google Scholar
  • Sherpa Romeo
  • Open J Gate
  • Genamics JournalSeek
  • Academic Keys
  • JournalTOCs
  • Ulrich's Periodicals Directory
  • Electronic Journals Library
  • RefSeek
  • Hamdard University
  • OCLC- WorldCat
  • Scholarsteer
  • SWB online catalog
  • Virtual Library of Biology (vifabio)
  • Publons
  • Euro Pub
Share This Page