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Article

Key residues in the nicotinic acetylcholine receptor β2 subunit contribute to α-conotoxin LvIA binding.

The Journal of biological chemistry - 10 Apr 2015

Zhangsun Dongting, Zhu Xiaopeng, Wu Yong, Hu Yuanyan, Kaas Quentin, Craik David J, McIntosh J Michael, Luo Sulan

Abstract excerpt

α-Conotoxin LvIA (α-CTx LvIA) is a small peptide from the venom of the carnivorous marine gastropod Conus lividus and is the most selective inhibitor of α3β2 nicotinic acetylcholine receptors (nAChRs) known to date. It can distinguish the α3β2 nAChR subtype from the α6β2* (* indicates the other subunit) and α3β4 nAChR subtypes. In this study, we performed mutational studies to assess the influence of residues of...

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Identifiers

PMID: 25713061
DOI: 10.1074/jbc.M114.632646
PMCID: PMC4392282

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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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