PH-induced conformational change of the influenza M2 protein C-terminal domain.
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ABSTRACT:
SUBMITTER: Nguyen PA
PROVIDER: S-EPMC2746938 | biostudies-other | 2008 Sep
REPOSITORIES: biostudies-other
Publications
pH-induced conformational change of the influenza M2 protein C-terminal domain.
Nguyen Phuong A PA Soto Cinque S CS Polishchuk Alexei A Caputo Gregory A GA Tatko Chad D CD Ma Chunlong C Ohigashi Yuki Y Pinto Lawrence H LH DeGrado William F WF Howard Kathleen P KP
Biochemistry 20080829 38
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 arra ...[more]
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