Send to:

Choose Destination
See comment in PubMed Commons below
Biochemistry. 2008 Sep 23;47(38):9934-6. doi: 10.1021/bi801315m. Epub 2008 Aug 29.

pH-induced conformational change of the influenza M2 protein C-terminal domain.

Author information

  • 1Department of Chemistry and Biochemistry, Swarthmore College, Swarthmore, Pennsylvania 19081, USA.


The M2 protein from influenza A is a pH-activated proton channel that plays an essential role in the viral life cycle and serves as a drug target. Using spin labeling EPR spectroscopy, we studied a 38-residue M2 peptide spanning the transmembrane region and its C-terminal extension. We obtained residue-specific environmental parameters under both high- and low-pH conditions for nine consecutive C-terminal sites. The region forms a membrane surface helix at both high and low pH, although the arrangement of the monomers within the tetramer changes with pH. Both electrophysiology and EPR data point to a critical role for residue Lys 49.

[PubMed - indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for American Chemical Society Icon for PubMed Central
    Loading ...
    Write to the Help Desk