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Molecular docking; modelling antibody-antigen interaction; hepatitis B virus B-cell epitope antigen; hepatitis B neutralizing monoclonal antibody; homology modelling; antigen-antibody docking.

The interaction of pres1 region of hepatitis B virus B-cell epitope antigen with specific hepatitis B neutralizing monoclonal antibody was examined by docking study. We modelled the 3D complex structure of B-cell epitope antigen residues CTTPAQGNSMFPSCCCTKPTDGNCY by homology modelling and docked it with the crystal structure of monoclonal antibody specific for the pres1 region of the hepatitis B virus. At the optimized docked conformation, the interactions between the amino acids of antigen and antibody were examined. It is found that the docked complex is stabilized by 59.3 kcal/mol. The stability of the docked antigen-antibody complex is due to hydrogen bonding and van der Waals interactions. The amino acids of the antigen and antibody responsible for the interaction were identified.

R Rajkannan¹ E J Padma Malar²

1. Department of Physical Chemistry, University of Madras, Guindy Campus, Chennai 600 025
2. National Centre for Ultrafast Processes, University of Madras, Taramani Campus, Chennai 600 113

Published

September 2007

Manuscript received

15 June 2007

Accepted

7 July 2007