Understanding the structural and energetic basis of inhibitor and substrate bound to the full-length NS3/4A: insights from molecular dynamics simulation, binding free energy calculation and network analysis.

@article{Xue2012UnderstandingTS,
  title={Understanding the structural and energetic basis of inhibitor and substrate bound to the full-length NS3/4A: insights from molecular dynamics simulation, binding free energy calculation and network analysis.},
  author={Weiwei Xue and Meixia Wang and Xiaojie Jin and Huanxiang Liu and Xiaojun Yao},
  journal={Molecular bioSystems},
  year={2012},
  volume={8 10},
  pages={2753-65}
}
Hepatitis C virus (HCV) bifunctional NS3/4A is an attractive anti-HCV drug target, as both the protease and helicase functions are required for viral infection and replication. Although the first generation of NS3/4A protease inhibitors (PIs) has focused almost exclusively on the interaction with the protease domain alone, recent studies have shown that PIs also inhibit the full-length NS3/4A protein. However, the detailed molecular mechanism of the interaction between protease inhibitors, as… CONTINUE READING
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