Structural and dynamic mechanisms for the function and inhibition of the M2 proton channel from influenza A virus

Jun Wang, Jade Xiaoyan Qiu, Cinque Soto, William F. Degrado

Research output: Contribution to journalArticle

89 Citations (Scopus)

Abstract

The M2 proton channel from influenza A virus, a prototype for a class of viral ion channels known as viroporins, conducts protons along a chain of water molecules and ionizable sidechains, including His37. Recent studies highlight a delicate interplay between protein folding, proton binding, and proton conduction through the channel. Drugs inhibit proton conduction by binding to an aqueous cavity adjacent to M2's proton-selective filter, thereby blocking access of proton to the filter, and altering the energetic landscape of the channel and the energetics of proton-binding to His37.

Original languageEnglish (US)
Pages (from-to)68-80
Number of pages13
JournalCurrent Opinion in Structural Biology
Volume21
Issue number1
DOIs
StatePublished - Feb 2011
Externally publishedYes

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Influenza A virus
Protons
Protein Folding
Ion Channels
Water
Pharmaceutical Preparations

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

Cite this

Structural and dynamic mechanisms for the function and inhibition of the M2 proton channel from influenza A virus. / Wang, Jun; Qiu, Jade Xiaoyan; Soto, Cinque; Degrado, William F.

In: Current Opinion in Structural Biology, Vol. 21, No. 1, 02.2011, p. 68-80.

Research output: Contribution to journalArticle

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