Cryo-EM Structure of the Open Human Ether-à-go-go-Related K+ Channel hERG

• Published in: Cell Vol. 169; no. 3; pp. 422 - 430.e10
• Main Authors: Wang, Weiwei, MacKinnon, Roderick
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 20.04.2017
• Subjects: action potentials; Amino Acid Sequence; arrhythmia; chemical structure; cryo-electron microscopy; cryo-EM; Cryoelectron Microscopy; drug-induced Long QT; drugs; ERG1 Potassium Channel - chemistry; ERG1 Potassium Channel - isolation & purification; ERG1 Potassium Channel - metabolism; ERG1 Potassium Channel - ultrastructure; hERG; hERG block; Humans; hydrophobicity; inactivation; K+ channel; Models, Molecular; mutation; potassium channels; Protein Conformation; Sequence Alignment; structure; voltage-dependent gating; K+ channel; drug-induced Long QT; hERG; voltage-dependent gating; inactivation; hERG block; cryo-EM; structure; K(+) channel

The human ether-à-go-go-related potassium channel (hERG, Kv11.1) is a voltage-dependent channel known for its role in repolarizing the cardiac action potential. hERG alteration by mutation or pharmacological inhibition produces Long QT syndrome and the lethal cardiac arrhythmia torsade de pointes. W...