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

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.

SUBMITTER: Nguyen PA 

PROVIDER: S-EPMC2746938 | biostudies-literature | 2008 Sep

REPOSITORIES: biostudies-literature