Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

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.

Type

Journal article

Journal

Curr Biol

Publication Date

11/03/1999

Volume

9

Pages

R173 - R175

Keywords

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