Structural basis for proton conduction and inhibition by the influenza M2 protein.

ABSTRACT: The influenza M2 protein forms an acid-activated and drug-sensitive proton channel in the virus envelope that is important for the virus lifecycle. The functional properties and high-resolution structures of this proton channel have been extensively studied to understand the mechanisms of proton conduction and drug inhibition. We review biochemical and electrophysiological studies of M2 and discuss how high-resolution structures have transformed our understanding of this proton channel. Comparison of structures obtained in different membrane-mimetic solvents and under different pH using X-ray crystallography, solution NMR, and solid-state NMR spectroscopy revealed how the M2 structure depends on the environment and showed that the pharmacologically relevant drug-binding site lies in the tr

SUBMITTER: Hong M 

PROVIDER: S-EPMC3527700 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature