Article
Studying the roles of W86, E202, and Y337 in binding of acetylcholine to acetylcholinesterase using a combined molecular dynamics and multiple docking approach.
Protein science : a publication of the Protein Society - 1 Dec 2003
Kua Jeremy, Zhang Yingkai, Eslami Angelique C, Butler John R, McCammon J Andrew
Abstract excerpt
A combined molecular dynamics simulation and multiple ligand docking approach is applied to study the roles of the anionic subsite residues (W86, E202, Y337) in the binding of acetylcholine (ACh) to acetylcholinesterase (AChE). We find that E202 stabilizes docking of ACh via electrostatic interactions. However, we find no significant electrostatic contribution from the aromatic residues. Docking energies of ACh...
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