Metal Bridge in S4 Segment Supports Helix Transition in Shaker Channel.

ABSTRACT: Voltage-gated ion channels play important roles in physiological processes, especially in excitable cells, in which they shape the action potential. In S4-based voltage sensors voltage-gated channels, a common feature is shared; the transmembrane segment 4 (S4) contains positively charged residues intercalated by hydrophobic residues. Although several advances have been made in understating how S4 moves through a hydrophobic plug upon voltage changes, the possible helix transition from α- to 3₁₀-helix in S4 during the activation process is still unresolved. Here, we have mutated several hydrophobic residues from I360 to F370 in the S4 segment into histidine, in i, i + 3 and i, i + 6 or i, i + 4 and i, i + 7 pairs, to favor 3₁₀- or α-helical conformations, respectively

SUBMITTER: Bassetto CAZ 

PROVIDER: S-EPMC7037500 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature