Luminal and non-luminal non-competitive inhibitor binding sites on the nicotinic acetylcholine receptor

摘要: SummaryThe nicotinic acetylcholine receptor presents two very well differentiated domains for ligand binding that account different cholinergic properties. In the hydrophilic extracellular region of α subunit exist sites agonists such as neurotransmitter acetylcholine, which upon trigger channel opening, and competitive antagonists d-tubocurarine, compete former inhibiting its pharmacological action. For non-competitive inhibitors, a population low-affinity have been found at lipid protein interface receptor. addition, M2 transmembrane domain, several high-affinity inhibitors chlorpromazine, triphenylmethylphosphonium, local anaesthetic QX-222 hydrophobic probe trifluoromethyl-iodophenyldiazirine. They are known luminal sites. Although meproadifen seems to be located between the...