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A combination of crystallographic and mutagenesis studies on the HERG K+ channel, a key determinant of cardiac excitability, has suggested how the protein's extramembraneous amino-terminal domain might act as a 'molecular brake' that slows down channel deactivation.


Journal article


Curr Biol

Publication Date





R173 - R175


Animals, Binding Sites, Cation Transport Proteins, DNA-Binding Proteins, ERG1 Potassium Channel, Ether-A-Go-Go Potassium Channels, Humans, Ion Channels, Long QT Syndrome, Potassium Channels, Potassium Channels, Voltage-Gated, Protein Conformation, Structure-Activity Relationship, Trans-Activators, Transcriptional Regulator ERG