Coupling between an electrostatic network and the Zn²⁺ binding site modulates Hv1 activation.

ABSTRACT: The voltage sensor (VS) domain in Hv1 proton channels mediates a voltage-dependent and H⁺-selective "aqueous" conductance (G_AQ) that is potently modulated by extracellular Zn²⁺ Although two conserved His residues are required for Zn²⁺ effects on G_AQ gating, the atomic structure of the Zn²⁺ coordination site and mechanism by which extracellular Zn²⁺ stabilizes a closed-state conformation remain unknown. Here we use His mutagenesis to identify residues that increase Zn²⁺ potency and are therefore likely to participate in first solvation shell interactions with Zn²⁺ Experimental Zn²⁺-mapping data were then used to constrain the structure of a new resting-state Hv1 model (Hv1 F). Molec

SUBMITTER: De La Rosa V 

PROVIDER: S-EPMC5987874 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature