Proton-Induced Conformational and Hydration Dynamics in the Influenza A M2 Channel.

ABSTRACT: The influenza A M2 protein is an acid-activated proton channel responsible for acidification of the inside of the virus, a critical step in the viral life cycle. This channel has four central histidine residues that form an acid-activated gate, binding protons from the outside until an activated state allows proton transport to the inside. While previous work has focused on proton transport through the channel, the structural and dynamic changes that accompany proton flux and enable activation have yet to be resolved. In this study, extensive Multiscale Reactive Molecular Dynamics simulations with explicit Grotthuss-shuttling hydrated excess protons are used to explore detailed molecular-level interactions that accompany proton transport in the +0, + 1, and +2 histidine charge states. The

SUBMITTER: Watkins LC 

PROVIDER: S-EPMC6768079 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature