PubMed 22522181
Referenced in: none
Automatically associated channels: Kv10.1 , Kv11.1 , Slo1
Title: HERG potassium channel regulation by the N-terminal eag domain.
Authors: Ahleah S Gustina, Matthew C Trudeau
Journal, date & volume: Cell. Signal., 2012 Aug , 24, 1592-8
PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/22522181
Abstract
Human ether-á-go-go related gene (hERG, K(v)11.1) potassium channels play a significant role in cardiac excitability. Like other K(v) channels, hERG is activated by membrane voltage; however, distinct from other K(v) channels, hERG channels have unusually slow kinetics of closing (deactivation). The mechanism for slow deactivation involves an N-terminal "eag domain" which comprises a PAS (Per-Arnt-Sim) domain and a short Cap domain. Here we review recent advances in understanding how the eag domain regulates deactivation, including several new Nuclear Magnetic Resonance (NMR) solution structures of the eag domain, and evidence showing that the eag domain makes a direct interaction with the C-terminal C-linker and Cyclic Nucleotide-Binding Homology Domain.