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Article

Direct gating of ATP-activated ion channels (P2X2 receptors) by lipophilic attachment at the outer end of the second transmembrane domain.

The Journal of biological chemistry - 10 Jan 2014

Rothwell Simon W, Stansfeld Phillip J, Bragg Laricia, Verkhratsky Alexej, North R Alan

Abstract excerpt

The ionic pore of the P2X receptor passes through the central axis of six transmembrane (TM) helices, two from each of three subunits. Val(48) and Ile(328) are at the outer end of TM1 and TM2, respectively. Homology models of the open and closed states of P2X2 indicate that pore opening is associated with a large lateral displacement of Ile(328). In addition, molecular dynamics simulations suggest that lipids...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 24273165
DOI: 10.1074/jbc.M113.529099
PMCID: PMC3887190

Provenance

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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