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Kv Channel Gating Requires a Compatible S4-S5 Linker and Bottom Part of S6, Constrained by Non-interacting Residues
Voltage-dependent K+ channels transfer the voltage sensor movement into gate opening or closure through an electromechanical coupling. To test functionally whether an interaction between the S4-S5Expand
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Molecular mechanism for depolarization-induced modulation of Kv channel closure
Voltage-dependent potassium (Kv) channels provide the repolarizing power that shapes the action potential duration and helps control the firing frequency of neurons. The K+ permeation through theExpand
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Properties of deactivation gating currents in Shaker channels.
The charge versus voltage relation of voltage-sensor domains shifts in the voltage axis depending on the initial voltage. Here we show that in nonconducting W434F Shaker K(+) channels, a largeExpand
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Role of the S6 C‐terminus in KCNQ1 channel gating
Co‐assembly of KCNQ1 α‐subunits with KCNE1 β‐subunits results in the channel complex underlying the cardiac IKs current in vivo. Like other voltage‐gated K+ channels, KCNQ1 has a tetramericExpand
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A polyether biotoxin binding site on the lipid-exposed face of the pore domain of Kv channels revealed by the marine toxin gambierol
Gambierol is a marine polycyclic ether toxin belonging to the group of ciguatera toxins. It does not activate voltage-gated sodium channels (VGSCs) but inhibits Kv1 potassium channels by an unknownExpand
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The S4-S5 Linker of KCNQ1 Channels Forms a Structural Scaffold with the S6 Segment Controlling Gate Closure*
In vivo, KCNQ1 α-subunits associate with the β-subunit KCNE1 to generate the slowly activating cardiac potassium current (IKs). Structurally, they share their topology with other Kv channels andExpand
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Modulation of HERG gating by a charge cluster in the N-terminal proximal domain.
Human ether-a-go-go-related gene (HERG) potassium channels contribute to the repolarization of the cardiac action potential and display unique gating properties with slow activation and fastExpand
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Gating of Shaker-type Channels Requires the Flexibility of S6 Caused by Prolines*
The recent crystallization of a voltage-gated K+ channel has given insight into the structure of these channels but has not resolved the issues of the location and the operation of the gate. TheExpand
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Phosphatidylinositol-4,5-bisphosphate (PIP(2)) stabilizes the open pore conformation of the Kv11.1 (hERG) channel.
Phosphatidylinositol-4,5-bisphosphate (PIP(2)) is a phospholipid that has been shown to modulate several ion channels, including some voltage-gated channels like Kv11.1 (hERG). From a biophysicalExpand
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Being Flexible: The Voltage-Controllable Activation Gate of Kv Channels
Kv channels form voltage-dependent potassium selective pores in the outer cell membrane and are composed out of four α-subunits, each having six membrane-spanning α-helices (S1–S6). The α-subunitsExpand
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