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Title

Mutation and docking studies on NS2b-NS3 complex from yellow fever virus towards drug discovery

 

Authors

Prabhavathy Kannappan, SundaraBaalaji Narayanan*

 

Affiliation

Structural Biology Lab, Department of Bioinformatics, School of Life Sciences, Bharathiar University, Coimbatore 641046, India

 

Email

sundarabaalaji@gmail.com; sundarabaalaji@buc.edu.in *Corresponding author

 

Phone

91-422-2428285

 

Fax

91-422-2422387/2425706

 

Article Type

Hypothesis

 

Date

Received May 28, 2011; Accepted June 27, 2011; Published July 06, 2011

 

Abstract

Yellow fever virus is the causative agent of Yellow fever. The genome of the virus contains three structural and seven non-structural proteins. Of these seven non-structural proteins, NS2B-NS3 protein complex has protease activity required for viral replication. Predicting the 3D structure of this complex and studying the interaction of residues at the recognized catalytic triad of the complex is an integral part to understand the virus replication mechanism. In the present study, the structure was determined for NS2B-NS3 complex by Homology modeling and modeled structure was validated for its stability. Mutation studies at the residues His94, Asp118 and Ser176 revealed that Asp118-His94 bond played an important role in the structural stability of NS2B-NS3 complex. This indicates site-directed mutagenesis, controlling YFV replication, as one mechanism to design vaccine strains. Docking studies of the bioactive compounds at the active site of NS2B-NS3 complex also indicated 4-hydroxypanduratin A as potential lead compound for drug development. The theoretical models will further pave way to experimentally verify our mutation and docking studies, thus taking a lead in pharmacogenomics and drug development.

 

Keywords

site-directed mutagenesis, docking, NS2B-NS3 complex

 

Citation

Kannappan & Narayanan. Bioinformation 6(8): 303-306 (2011)
 

Edited by

P Kangueane

 

ISSN

0973-2063

 

Publisher

Biomedical Informatics

 

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.