How does huperzine A enter and leave the binding gorge of acetylcholinesterase? Steered molecular dynamics simulations.

@article{Xu2003HowDH,
  title={How does huperzine A enter and leave the binding gorge of acetylcholinesterase? Steered molecular dynamics simulations.},
  author={Yechun Xu and Jianhua Shen and Xiaomin Luo and Israel Silman and Joel L. Sussman and K. A. Chen and Hualiang Jiang},
  journal={Journal of the American Chemical Society},
  year={2003},
  volume={125 37},
  pages={11340-9}
}
The entering and leaving processes of Huperzine A (HupA) binding with the long active-site gorge of Torpedo californica acetylcholinesterase (TcAChE) have been investigated by using steered molecular dynamics simulations. The analysis of the force required along the pathway shows that it is easier for HupA to bind to the active site of AChE than to disassociate from it, which for the first time interprets at the atomic level the previous experimental result that unbinding process of HupA is… CONTINUE READING

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