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Article

An open-channel blocker interacts with adjacent turns of alpha-helices in the nicotinic acetylcholine receptor.

Neuron - 1 Jan 1990

Charnet P, Labarca C, Leonard R J, Vogelaar N J, Czyzyk L, Gouin A, Davidson N, Lester H A

Abstract excerpt

The binding site for an open-channel blocker, QX-222, at mouse muscle nicotinic acetylcholine receptors was probed using site-directed mutagenesis, oocyte expression, and electrophysiological analysis. The proposed cytoplasmic end of the M2 transmembrane helix is termed position 1'. At position 10' (alpha S252, beta T263, gamma A261, delta A266), Ala residues yield stronger and longer binding of QX-222 than Ser...

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PMID: 1690017
DOI: 10.1016/0896-6273(90)90445-l

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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