Voltage-dependent gating of KCNH potassium channels lacking a covalent link between voltage-sensing and pore domains

@inproceedings{Lrinczi2015VoltagedependentGO,
  title={Voltage-dependent gating of KCNH potassium channels lacking a covalent link between voltage-sensing and pore domains},
  author={{\'E}va L{\"o}rinczi and Juan Camilo G{\'o}mez-Posada and Pilar de la Pe{\~n}a and Adam P Tomczak and Jorge Fern{\'a}ndez-Trillo and Ulrike Leipscher and Walter Stuehmer and Francisco Barros and Luis A Pardo},
  booktitle={Nature communications},
  year={2015}
}
Voltage-gated channels open paths for ion permeation upon changes in membrane potential, but how voltage changes are coupled to gating is not entirely understood. Two modules can be recognized in voltage-gated potassium channels, one responsible for voltage sensing (transmembrane segments S1 to S4), the other for permeation (S5 and S6). It is generally assumed that the conversion of a conformational change in the voltage sensor into channel gating occurs through the intracellular S4-S5 linker… CONTINUE READING
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Structural basis of a Kv7.1 potassium channel gating module: studies of the intracellular C-terminal domain in complex with calmodulin

  • D Sachyani
  • Structure 22,
  • 2014

Opposite effects of the S4-S5 linker and PIP(2) on voltagegated channel function: KCNQ1/KCNE1 and other channels

  • Choveau, S F.
  • Front. Pharmacol. 3,
  • 2012

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