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Article

Distinct modulation of inactivation by a residue in the pore domain of voltage-gated Na+ channels: mechanistic insights from recent crystal structures.

Scientific reports - 12 Jan 2018

Cervenka Rene, Lukacs Peter, Gawali Vaibhavkumar S, Ke Song, Koenig Xaver, Rubi Lena, Zarrabi Touran, Hilber Karlheinz, Sandtner Walter, Stary-Weinzinger Anna, Todt Hannes

Abstract excerpt

Inactivation of voltage-gated Na+ channels (VGSC) is essential for the regulation of cellular excitability. The molecular rearrangement underlying inactivation is thought to involve the intracellular linker between domains III and IV serving as inactivation lid, the receptor for the lid (domain III S4-S5 linker) and the pore-lining S6 segements. To better understand the role of the domain IV S6 segment in...

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Identifiers

PMID: 29330525
DOI: 10.1038/s41598-017-18919-1
PMCID: PMC5766632

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

Source receipt: pubmed, retrieved 7 Sept 2026.

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