Nicotinic acetylcholine receptors are transmembrane
oligomeric proteins that mediate interconversions
between open and closed channel states under the
control of neurotransmitters.
In order to represent the functional properties of such
receptors, we have developed a kinetic model that links
conformational interconversion rates to agonist binding
and extends the general principles of the Monod-
Wyman-Changeux model of allosteric transitions.
Application of the model to the peripheral nicotinic acetylcholine receptor
(nAChR) accounts for the main properties of ligand-gating,
including single-channel events, and several new
relationships are predicted.
In terms of future developments, the analysis presented here provides
a physical basis for constructing more biologically realistic
models of synaptic modulation that may be applied to
artificial neural networks.
Edelstein SJ, Schaad O, Henry E, Bertrand D, Changeux JP (1996) A kinetic mechanism for nicotinic acetylcholine receptors based on multiple allosteric transitions. Biol Cybern 75:361-79 [PubMed]