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Article

Analysis of the pore structure of the influenza A virus M(2) ion channel by the substituted-cysteine accessibility method.

Journal of virology - 1 Sept 2000

Shuck K, Lamb R A, Pinto L H

Abstract excerpt

The M(2) ion channel of influenza A virus is a small integral membrane protein whose active form is a homotetramer with each polypeptide chain containing 96-amino-acid residues. To identify residues of the transmembrane (TM) domain that line the presumed central ion-conducting pore, a set of mutants was generated in which each residue of the TM domain (residues 25 to 44) was replaced by cysteine. The...

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Identifiers

PMID: 10933681
DOI: 10.1128/jvi.74.17.7755-7761.2000
PMCID: PMC112304

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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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