Febin Prabhu Dass J

Department of Integrative Biology

School of Bio Sciences and Technology

Vellore Campus

Jayanthi S

Department of Biotechnology

Bhavaniprasad V

Vellore Institute of Technology (VIT) is a private university located in&nbsp;Tamil Nadu, India. Founded in 1984, as Vellore Engineering College, the institution offers 20 undergraduate, 34 postgraduate, four integrated and four research programs. It has campuses in Vellore, Amravati, Bhopal and Chennai.

VIT is one of the top ranked private universities in India according to NIRF, THE and QS Rankings.&nbsp;Govt. of India has recognized&nbsp;VIT, Vellore as an&nbsp;Institution of Eminence. This has allowed VIT to take independent quality initiatives and move up in world ranking.

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VIT University

Molecular BioSystems

Activation mechanism of claudin-4 by ephrin type-A receptor 2: a molecular dynamics approach

Claudin-1 (CLDN1) in association with envelope glycoprotein (CD81) mediates the fusion of HCV into the cytosol. Recent studies have indicated that point mutations in CLDN1 are important for the entry of hepatitis C virus (HCV). To validate these findings, we employed a computational platform to investigate the structural effect of two point mutations (I32M and E48K). Initially, three-dimensional co-ordinates for CLDN1 receptor sequence were generated. Then, three mutant models were built using the point mutation including a double mutant (I32M/E48K) model from the native model structure. Finally, all the four model structures including the native and three mutant models were subjected to molecular dynamics (MD) simulation for a period of 25 ns to appreciate their dynamic behavior. The MD trajectory files were analyzed using cluster and principal component method. The analysis suggested that either of the single mutation has negligible effect on the overall structure of CLDN1 compared to the double mutant form. However, the double mutant model of CLDN1 shows significant negative impact through the impairment of H-bonds and the simultaneous increase in solvent accessible surface area. Our simulation results are visibly consistent with the experimental report suggesting that the CLDN1 receptor distortion is prominent due to the double mutation with large surface accessibility. This increase in accessible surface area due to the coexistence of double mutation may be presumed as one of the key factor that results in permissive action of HCV attachment and infection.

Journal of Biomolecular Structure and Dynamics

Insilico modeling and molecular dynamic simulation of claudin-1 point mutations in HCV infection

Biochimica et Biophysica Acta (BBA) - Biomembranes

Homology modeling of human CCR5 and analysis of its binding properties through molecular docking and molecular dynamics simulation

Molecular Systems Biology

Fast, scalable generation of high‐quality protein multiple sequence alignments using Clustal Omega

Nature Protocols

The HADDOCK web server for data-driven biomolecular docking

Journal	Data powered by TypesetMolecular BioSystems
Publisher	Data powered by TypesetRoyal Society of Chemistry (RSC)
ISSN	1742-206X
Open Access	0