Article
Acetylcholinesterase: mechanisms of covalent inhibition of wild-type and H447I mutant determined by computational analyses.
Journal of the American Chemical Society - 23 May 2007
Cheng Yuhui, Cheng Xiaolin, Radić Zoran, McCammon J Andrew
Abstract excerpt
The reaction mechanisms of two inhibitors TFK+ and TFK0 binding to both the wild-type and H447I mutant mouse acetylcholinesterase (mAChE) have been investigated by using a combined ab initio quantum mechanical/molecular mechanical (QM/MM) approach and classical molecular dynamics (MD) simulations. In the wild-type mAChE, the binding reactions of TFK+ and TFK0 are both spontaneous processes, which proceed through...
Topics
- Acetylcholinesterase
- Acylation
- Animals
- Binding Sites
- Computer Simulation
- Histidine
- Isoleucine
- Mice
- Models, Molecular
- Mutation
- Protein Structure, Tertiary