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Docking of B-cell epitope antigen to specific hepatitis B antibody |
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| Authors: | R Rajkannan and E J Padma Malar |
| Institution: | (1) Department of Physical Chemistry, University of Madras, Guindy Campus, Chennai, 600 025, India;(2) National Centre for Ultrafast Processes, University of Madras, Taramani Campus, Chennai, 600 113, India |
| Abstract: | 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. |
| Keywords: | Molecular docking modelling antibody-antigen interaction hepatitis B virus B-cell epitope antigen hepatitis B neutralizing monoclonal antibody homology modelling antigen-antibody docking |
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