Abstract
Upon first inspection, acetylcholinesterase (AChE) and the nicotinic acetylcholine receptor (nAchR) share several functional and structural characteristics. Both recognize the neurotransmitter, acetylcholine, and elicit the respective actions of catalysis of the neurotransmitter and neurotransmitter-induced channel opening in a millisecond time frame. Their relative stoichiometries at various synapses are carefully regulated within precise limits. Homologous toxins, the fasciculins and a-neurotoxins (i. e., α-cobratoxin and α-bungaro-toxin), which have nearly identical tertiary structures, inhibit the two respective proteins at concentrations in the picomolar to subpicomolar range. Finally, the two proteins show coordinated expression during development.
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Taylor, P., Radić, Z., Kreienkamp, HJ., Luo, Z., Pickering, N.A., Camp, S. (1995). Ligand Specificity and Gene Expression in the Cholinergic Synapse. In: Quinn, D.M., Balasubramanian, A.S., Doctor, B.P., Taylor, P. (eds) Enzymes of the Cholinesterase Family. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1051-6_3
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