Rapid binding of a cationic active site inhibitor to wild type and mutant mouse acetylcholinesterase: Brownian dynamics simulation including diffusion in the active site gorge.

@article{Tara1998RapidBO,
  title={Rapid binding of a cationic active site inhibitor to wild type and mutant mouse acetylcholinesterase: Brownian dynamics simulation including diffusion in the active site gorge.},
  author={Serge Tara and Adrian H. Elcock and Paul D. Kirchhoff and James M. Briggs and Zoran Radic and Paul Taylor and James Andrew McCammon},
  journal={Biopolymers},
  year={1998},
  volume={46 7},
  pages={465-74}
}
It is known that anionic surface residues play a role in the long-range electrostatic attraction between acetylcholinesterase and cationic ligands. In our current investigation, we show that anionic residues also play an important role in the behavior of the ligand within the active site gorge of acetylcholinesterase. Negatively charged residues near the gorge opening not only attract positively charged ligands from solution to the enzyme, but can also restrict the motion of the ligand once it… CONTINUE READING

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