Jp. Changeux et Sj. Edelstein, Allosteric mechanisms in normal and pathological nicotinic acetylcholine receptors, CUR OP NEUR, 11(3), 2001, pp. 369-377
Recent chemical and advanced structural studies on site-directed and natura
lly occurring pathological mutants of individual members of the multigene f
amily of nicotinic acetylcholine receptors have yielded structure-function
relationships supporting indirect 'allosteric' interactions between the ace
tylcholine-binding sites and the ion channel in signal transduction.