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Muscle-type nicotinic acetylcholine receptor (AChR) is the key signaling molecule in neuromuscular junctions. Here, we present the structures of full-length human adult receptors in complex with Fab35 in α-bungarotoxin (αBuTx)-bound resting states and ACh-bound desensitized states. In addition to identifying the conformational changes during recovery from desensitization, we also used electrophysiology to probe the effects of eight previously unstudied AChR genetic variants found in patients with congenital myasthenic syndrome (CMS), revealing they cause either slow- or fast-channel CMS characterized by prolonged or abbreviated ion channel bursts. The combined kinetic and structural data offer a better understanding of both the AChR state transition and the pathogenic mechanisms of disease variants.

Original publication

DOI

10.1016/j.celrep.2025.115581

Type

Journal

Cell Rep

Publication Date

17/04/2025

Volume

44

Keywords

CP: Molecular biology, CP: Neuroscience, acetylcholine receptor, congenital myasthenic syndromes, cryo-EM, electrophysiology, ion channel, neuromuscular junction, nicotinic receptor, pLGIC