Resonance assignment and secondary structure prediction of the N-terminal domain of hERG (Kv11.1).
The hERG (human ether-à-go-go related gene) channel is a member of the eag voltage-gated K(+) channel family. In common with other members of this family, it has a subunit topology of six trans-membrane helices that tetramerise to form a functional ion-channel. In addition, hERG has an N-terminal PAS (Per, Arnt and Sim) domain and a C-terminal cyclic nucleotide binding domain (cNBD). Both these cytosolic domains are involved in regulation of the gating of the ion channel as demonstrated by inheritable mutations in these domains that result in either a loss, or a gain, in function. Here we report near complete backbone and side chain (15)N, (13)C and (1)H assignments for the N-terminal domain (residues 1-135) including the functionally critical first 26 residues. Comparison with the secondary structure of the crystal structure (residues 26-135) suggests that the solution and crystal structures are very similar except that the solution structure contains an additional helix between residues 12-23; a region of the protein important for channel gating.
Muskett
Frederick W
FW
Department of Biochemistry, University of Leicester, United Kingdom. fwm1@le.ac.uk
Mitcheson
John S
JS
D000595:Amino Acid Sequence; D051638:Ether-A-Go-Go Potassium Channels / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
D051638:Ether-A-Go-Go Potassium Channels; C496884:KCNH1 protein, human