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Insight into the Mechanism of the Influenza A Proton Channel from a Structure in a Lipid Bilayer

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Science  22 Oct 2010:
Vol. 330, Issue 6003, pp. 509-512
DOI: 10.1126/science.1191750

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M2 Out of the Envelope

The M2 protein from influenza A virus forms an acid-activated tetrameric proton channel in the viral envelope and is essential for viral replication. Two manuscripts shed light on the functional mechanism of this channel. Sharma et al. (p. 509; see the Perspective by Fiorin et al.) determined the structure of the conductance domain in a lipid bilayer and propose that a histidine and tryptophan from each monomer form a cluster that guides protons through the channel in a mechanism that involves forming and breaking hydrogen bonds between adjacent pairs of histidines. Hu et al. (p. 505; see the Perspective by Fiorin et al.) focused on the structure and dynamics of the proton-selective histidine at high and low pH, proposing that proton conduction involves histidine deprotonation and reprotonation.

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