Voltage-dependent structural models of the human Hv1 proton channel from long-timescale molecular dynamics simulations.

ABSTRACT: The voltage-gated Hv1 proton channel is a ubiquitous membrane protein that has roles in a variety of cellular processes, including proton extrusion, pH regulation, production of reactive oxygen species, proliferation of cancer cells, and increased brain damage during ischemic stroke. A crystal structure of an Hv1 construct in a putative closed state has been reported, and structural models for the channel open state have been proposed, but a complete characterization of the Hv1 conformational dynamics under an applied membrane potential has been elusive. We report structural models of the Hv1 voltage-sensing domain (VSD), both in a hyperpolarized state and a depolarized state resulting from voltage-dependent conformational changes during a 10-μs-timescale atomistic molecular dynamics simul

SUBMITTER: Geragotelis AD 

PROVIDER: S-EPMC7306757 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature