Article
Site-directed mutants designed to test back-door hypotheses of acetylcholinesterase function.
FEBS letters - 13 May 1996
Faerman C, Ripoll D, Bon S, Le Feuvre Y, Morel N, Massoulié J, Sussman J L, Silman I
Abstract excerpt
The location of the active site of the rapid enzyme, acetylcholinesterase, near the bottom of a deep and narrow gorge indicates that alternative routes may exist for traffic of substrate, products or solute into and out of the gorge. Molecular dynamics suggest the existence of a shutter-like back door near Trp84, a key- residue in the binding site for acetylcholine, in the Torpedo californica enzyme. The homology...
Topics
- Acetylcholinesterase
- Animals
- Base Sequence
- Binding Sites
- Cells, Cultured
- Computer Simulation
- Disulfides
- Enzyme Activation
- Kidney
- Models, Molecular
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Protein Conformation