Referenced in: none

Automatically associated channels: Kv11.1

Title: 1H, 13C and 15N chemical shift assignments for the N-terminal domain of the voltage-gated potassium channel-hERG.

Authors: Qingxin Li, Manfred Raida, Congbao Kang

Journal, date & volume: Biomol NMR Assign, 2010 Oct , 4, 211-3

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/20607461

Abstract
The human ether à go-go related gene (hERG) voltage-gated potassium controls the rapid delayed rectifier potassium current (I(ks)) in heart. The N-terminal 135 amino acids (NTD) form a Per-Arnt-Sim (PAS) domain which involves in signal transduction and protein-protein interactions. NTD was shown to be necessary for the regulation of the channel activity through its interaction with the channel pore region of hERG. Mutations in NTD were related to serious heart diseases. We report the (1)H, (13)C and (15)N chemical shift assignments for NTD using 2D and 3D heteronuclear NMR experiments. More than 95% backbone resonance assignments were obtained.