Acetylcholinesterase: Structure and use as a model for specific cation-protein interactions

@article{Sussman1992AcetylcholinesteraseSA,
  title={Acetylcholinesterase: Structure and use as a model for specific cation-protein interactions},
  author={Joel L. Sussman and Israel Silman},
  journal={Current Biology},
  year={1992},
  volume={2}
}
Acetylcholinesterase is an 0t/J3 protein with an overall fold very similar to several hydrolytic enzymes of widely differing phylogenetic origin and catalytic function. The structure reveals, for the first time, a binding pocket for the neurotransmitter acetylcholine. The catalytic triad lies near the bottom of a deep and narrow gorge, lined with aromatic amino acids. The positive quaternary group in acetylcholine and other cholinergic ligands makes close contact with aromatic residues; thus… CONTINUE READING
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