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Article

Structure and dynamics of the proton-selective histidine and the gating tryptophan in an inward rectifying hybrid influenza B and A virus M2 proton channel.

Physical chemistry chemical physics : PCCP - 31 Jul 2024

Pankratova Yanina, McKay Matthew J, Ma Chunlong, Tan Haozhou, Wang Jun, Hong Mei

Abstract excerpt

The M2 proteins of influenza A and B viruses form acid-activated proton channels that are essential for the virus lifecycle. Proton selectivity is achieved by a transmembrane (TM) histidine whereas gating is achieved by a tryptophan residue. Although this functional apparatus is conserved between AM2 and BM2 channels, AM2 conducts protons exclusively inward whereas BM2 conducts protons in either direction...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 39037444
DOI: 10.1039/d4cp01648c
PMCID: PMC11290064

Provenance

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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