1H, 13C and 15N chemical shift assignments for the N-terminal domain of the voltage-gated potassium channel-hERG.
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.
Li
Qingxin
Q
Institute of Biotechnology and Nanotechnology, The Agency for Science, Technology and Research, Singapore, 138669, Singapore.
Raida
Manfred
M
Kang
CongBao
C
D000595:Amino Acid Sequence; D002247:Carbon Isotopes; D000072237:ERG1 Potassium Channel; D051638:Ether-A-Go-Go Potassium Channels / Q000737:chemistry*; D006801:Humans; D006859:Hydrogen; D015640:Ion Channel Gating; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
D002247:Carbon Isotopes; D000072237:ERG1 Potassium Channel; D051638:Ether-A-Go-Go Potassium Channels; C000606913:KCNH2 protein, human; D009587:Nitrogen Isotopes; D006859:Hydrogen