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

Phuong A. Nguyen, Cinque S. Soto, Alexei Polishchuk, Gregory A. Caputo, Chad D. Tatko, Chunlong Ma, Yuki Ohigashi, Lawrence H. Pinto, William F. Degrado, Kathleen P. Howard

Research output: Contribution to journalArticlepeer-review

60 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)9934-9936
Number of pages3
Issue number38
StatePublished - Sep 23 2008
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry


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