pH-Induced Conformational Change of the Influenza M2 Protein C-Terminal Domain
- 29 August 2008
- journal article
- other
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 47 (38) , 9934-9936
- https://doi.org/10.1021/bi801315m
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.Keywords
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