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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

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

Abstract

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.

PMID:
18754675
PMCID:
PMC2746938
DOI:
10.1021/bi801315m
[Indexed for MEDLINE]
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