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Article

Functional studies and modeling of pore-lining residue mutants of the influenza a virus M2 ion channel.

Biochemistry - 2 Feb 2010

Balannik Victoria, Carnevale Vincenzo, Fiorin Giacomo, Levine Benjamin G, Lamb Robert A, Klein Michael L, Degrado William F, Pinto Lawrence H

Abstract excerpt

The A/M2 protein of influenza A virus forms a tetrameric proton-selective pH-gated ion channel. The H(37)xxxW(41) motif located in the channel pore is responsible for its gating and proton selectivity. Channel activation most likely involves protonation of the H37 residues, while the conductive state of the channel is characterized by two or three charged His residues in a tetrad. A/M2 channel activity is...

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Identifiers

PMID: 20028125
DOI: 10.1021/bi901799k
PMCID: PMC4924815

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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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