Ontology highlight
ABSTRACT:
SUBMITTER: Haitin Y
PROVIDER: S-EPMC2275789 | biostudies-literature | 2008
REPOSITORIES: biostudies-literature
Haitin Yoni Y Yisharel Ilanit I Malka Eti E Shamgar Liora L Schottelndreier Hella H Peretz Asher A Paas Yoav Y Attali Bernard B
PloS one 20080409 4
Voltage-gated K(+) channels comprise a central pore enclosed by four voltage-sensing domains (VSDs). While movement of the S4 helix is known to couple to channel gate opening and closing, the nature of S4 motion is unclear. Here, we substituted S4 residues of Kv7.1 channels by cysteine and recorded whole-cell mutant channel currents in Xenopus oocytes using the two-electrode voltage-clamp technique. In the closed state, disulfide and metal bridges constrain residue S225 (S4) nearby C136 (S1) wit ...[more]