Trp207 regulation of voltage-dependent activation of human H_v1 proton channel.

ABSTRACT: In voltage-gated Na⁺ and K⁺ channels, the hydrophobicity of noncharged residues in the S4 helix has been shown to regulate the S4 movement underlying the process of voltage-sensing domain (VSD) activation. In voltage-gated proton channel H_v1, there is a bulky noncharged tryptophan residue located at the S4 transmembrane segment. This tryptophan remains entirely conserved across all H_v1 members but is not seen in other voltage-gated ion channels, indicating that the tryptophan contributes different roles in VSD activation. The conserved tryptophan of human voltage-gated proton channel H_v1 is Trp207 (W207). Here, we showed that W207 modifies human H_v1 voltage-dependent activation, and small residues replacement at position 207

SUBMITTER: Zhang L 

PROVIDER: S-EPMC10875263 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature