Abstract
The HERG K+ channel has very unusual kinetic behaviour that includes slow activation but rapid inactivation. These features are critical for normal cardiac repolarisation as well as in preventing lethal ventricular arrhythmias. Extensive mutagenesis of the HERG K+ channel has allowed identification of which regions of the channel are important for the unusual kinetic behaviour of the channel. Furthermore, structural studies on scorpion toxins that potently inhibit HERG are beginning to provide clues as to the structural differences between HERG and other voltage-gated K+ channels.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Amino Acid Sequence
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Animals
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Cell Membrane / drug effects
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Cell Membrane / physiology*
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ERG1 Potassium Channel
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Ether-A-Go-Go Potassium Channels
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Humans
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Ion Channel Gating / drug effects
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Ion Channel Gating / physiology*
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Kinetics
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Membrane Potentials / drug effects
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Membrane Potentials / physiology
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Models, Molecular*
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Molecular Sequence Data
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Potassium / metabolism*
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Potassium Channels, Voltage-Gated / chemistry*
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Potassium Channels, Voltage-Gated / physiology*
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Protein Conformation
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Scorpion Venoms / chemistry
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Scorpion Venoms / pharmacology*
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Structure-Activity Relationship
Substances
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ERG1 Potassium Channel
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Ether-A-Go-Go Potassium Channels
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KCNH2 protein, human
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Potassium Channels, Voltage-Gated
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Scorpion Venoms
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Potassium