pH-Induced Conformational Change Of The Influenza M2 Protein C-Terminal Domain
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 reo,ion 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.
Phuong Anh Nguyen , '07; C. S. Soto; A. Polishchuk; G. A. Caputo; C. D. Tatko; C. Ma; Y. Ohigashi; L. H. Pinto; W. F. DeGrado; and Kathleen P. Howard.
"pH-Induced Conformational Change Of The Influenza M2 Protein C-Terminal Domain".
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