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Article

Structural and functional studies of the modulator NS9283 reveal agonist-like mechanism of action at α4β2 nicotinic acetylcholine receptors.

The Journal of biological chemistry - 5 Sept 2014

Olsen Jeppe A, Ahring Philip K, Kastrup Jette S, Gajhede Michael, Balle Thomas

Abstract excerpt

Modulation of Cys loop receptor ion channels is a proven drug discovery strategy, but many underlying mechanisms of the mode of action are poorly understood. We report the x-ray structure of the acetylcholine-binding protein from Lymnaea stagnalis with NS9283, a stoichiometry selective positive modulator that targets the α4-α4 interface of α4β2 nicotinic acetylcholine receptors (nAChRs). Together with homology...

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Identifiers

PMID: 24982426
DOI: 10.1074/jbc.M114.568097
PMCID: PMC4155659

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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