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Article

The pore structure and gating mechanism of K2P channels.

The EMBO journal - 5 Aug 2011

Piechotta Paula L, Rapedius Markus, Stansfeld Phillip J, Bollepalli Murali K, Ehrlich Gunter, Erhlich Gunter, Andres-Enguix Isabelle, Fritzenschaft Hariolf, Decher Niels, Sansom Mark S P, Tucker Stephen J, Baukrowitz Thomas

Abstract excerpt

Two-pore domain (K2P) potassium channels are important regulators of cellular electrical excitability. However, the structure of these channels and their gating mechanism, in particular the role of the bundle-crossing gate, are not well understood. Here, we report that quaternary ammonium (QA) ions bind with high-affinity deep within the pore of TREK-1 and have free access to their binding site before channel...

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Identifiers

PMID: 21822218
DOI: 10.1038/emboj.2011.268
PMCID: PMC3181484

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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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