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Article

Molecular interactions involved in proton-dependent gating in KcsA potassium channels.

The Journal of general physiology - 1 Dec 2013

Posson David J, Thompson Ameer N, McCoy Jason G, Nimigean Crina M

Abstract excerpt

The bacterial potassium channel KcsA is gated open by the binding of protons to amino acids on the intracellular side of the channel. We have identified, via channel mutagenesis and x-ray crystallography, two pH-sensing amino acids and a set of nearby residues involved in molecular interactions that influence gating. We found that the minimal mutation of one histidine (H25) and one glutamate (E118) near the...

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Identifiers

PMID: 24218397
DOI: 10.1085/jgp.201311057
PMCID: PMC3840921

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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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