Acetylcholinesterase (AChE) is an enzyme composed of 531 residues, that often appears in humans as a dimer(2). AChE catalyses the breakdown of the neurotransmitter Acetylcholine by hydrolysis(3). This occurs at the neuromuscular junction and is important for the termination of synaptic transmission(2,3). However AChE also has other roles in structural processes, cell differentiation and synaptogenesis(1). This paper investigates the concept that AChE can experience allosteric effects. Allostery is the regulation of enzyme activity via the binding of another molecule at a site other than the active site. This paper outlines the discovery of new allosteric sites (referred to as “Site 2” and “Site 3”), which were used to discover new allosteric inhibitors of AChE. These are useful for investigating the non-cholinergic functions of AChE and may have important pharmacological applications(1).
PDB file: 3LII References (PMID): 29873262; 20138030; 24179466.
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