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}
}
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Crystal structure of an acetylcholinesterase-fasciculin complex: interaction of a three-fingered toxin from snake venom with its target.
Fasciculin: modification of carboxyl groups and discussion of structure-activity relationship.
Structure and dynamics of the active site gorge of acetylcholinesterase: Synergistic use of molecular dynamics simulation and X‐ray crystallography
TLDR
Simulation of the active site of acetylcholinesterase from Torpedo californica suggests that a bis‐quaternary decamethonium (DECA) ion, acquired during enzyme purification, resides in the gorge and appears to stabilize part of the gorge wall through electrostatic interactions.
Understanding the structure and function of catalases: clues from molecular evolution and in vitro mutagenesis.
Characterization of the interaction between acetylcholinesterase and laminin : a template for discovering redundancy
TLDR
The results define the interaction sites involved in the AChE-laminin interaction and suggest that the interaction plays a role in cell adhesion.
Characterization of Acetylcholinesterase from Various Sources: A Mini Re
TLDR
In this review, various aspects of acetylcholinesterase (AChE) are reviewed and it is assumed to participate in the growth and development and to scavenge the cholinergic toxins, and to have an auxiliary role in synaptic transmission.
Peripheral binding site is involved in the neurotrophic activity of acetylcholinesterase.
TLDR
The PAS domain of AChE is involved in the neurotrophic activity of the enzyme, which was abolished by propidium and gallamine, two peripheral anionic binding site (PAS) ligands.
The cyanobacterial alkaloid nostocarboline: an inhibitor of acetylcholinesterase and trypsin
TLDR
Nostocarboline is the first described cyanobacterial serine protease inhibitor of an alkaloid structure and its potential as a lead compound for the development of useful therapeutic AChE inhibitors is discussed.
Acetylcholinesterase Accelerates Assembly of Amyloid-β-Peptides into Alzheimer's Fibrils: Possible Role of the Peripheral Site of the Enzyme
Insensitive Acetylcholinesterase as Sites for Resistance to Organophosphates and Carbamates in Insects: Insensitive Acetylcholinesterase Confers Resistance in Lepidoptera
TLDR
Vertebrates and arthropods have only one enzyme which, whilst containing characteristics of both, is generally considered to be AChE (Toutant 1989); however, Vertebrate species possess acetylcholinesterase and butyrylcholiersterase, differentiated by substrate preferences.
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References

SHOWING 1-10 OF 27 REFERENCES
Acetylcholine interactions with tryptophan‐184 of the α‐subunit of the nicotinic acetylcholine receptor revealed by transferred nuclear Overhauser effect
Allosteric transitions of the acetylcholine receptor probed at the amino acid level with a photolabile cholinergic ligand.
  • J. Galzi, F. Revah, J. Changeux
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1991
Structural changes occurring upon desensitization of the Torpedo marmorata acetylcholine receptor were monitored with tritiated p-(N,N-dimethyl)aminobenzenediazonium fluoroborate, a reversible…
On the specificity of antibody/antigen interactions: phosphocholine binding to McPC603 and the correlation of three-dimensional structure and sequence data.
Structure of the agonist-binding site of the nicotinic acetylcholine receptor. [3H]acetylcholine mustard identifies residues in the cation-binding subsite.
Onchidal: a naturally occurring irreversible inhibitor of acetylcholinesterase with a novel mechanism of action.
TLDR
Onchidal can be found in several different species of Onchidella and it is toxic to fish, and this novel toxin could potentially be exploited in the design of a new class of anticholinesterase insecticides and in the identification of amino acids that contribute to the binding and hydrolysis of acetylcholine.
Mapping and modification of an antibody hapten binding site: a site-directed mutagenesis study of McPC603.
TLDR
The quantitative contributions of various amino acid residues to hapten binding in the Fv fragment of the antibody McPC603 were investigated by site-directed mutagenesis and may serve as the basis for the development of quantitative treatments of antigen-antibody interactions.
Muscarinic acetylcholine receptors. Peptide sequencing identifies residues involved in antagonist binding and disulfide bond formation.
Tacrine: A pharmacological review
Acetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition states
New insights into the structure and function of potassium channels
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