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Nicotinic ACh receptor (nAChR) α4 and t2 subunits assemble in two alternate stoichiornetries to produce (α4β2)2α4 and (α4β2)232, which display different agonist sensitivities.Functionallyrelevant, agonist binding sites are thought to be located at α4 (+)/β2 (-) subunit interfaces but because these interfaces are present in both receptor isoforms, it is unlikely that they account for differences in agonist sensitivities.