pH-Induced Conformational Change Of The Influenza M2 Protein C-Terminal Domain
Document Type
Article
Publication Date
9-23-2008
Published In
Biochemistry
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 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.
Recommended Citation
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.
(2008).
"pH-Induced Conformational Change Of The Influenza M2 Protein C-Terminal Domain".
Biochemistry.
Volume 47,
Issue 38.
9934-9936.
DOI: 10.1021/bi801315m
https://works.swarthmore.edu/fac-chemistry/51