NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker.

@article{Li2010NMRSS,
  title={NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker.},
  author={Qingxin Li and Shovanlal Gayen and Angela Shuyi Chen and Qiwei Huang and Manfred Roman Raida and Congbao Kang},
  journal={Biochemical and biophysical research communications},
  year={2010},
  volume={403 1},
  pages={
          126-32
        }
}
The human Ether-à-go-go Related Gene (hERG) potassium channel mediates the rapid delayed rectifier current (IKr) in the cardiac action potential. Mutations in the 135 amino acid residue N-terminal domain (NTD) cause channel dysfunction or mis-translocation. To study the structure of NTD, it was overexpressed and purified from Escherichia coli cells using affinity purification and gel filtration chromatography. The purified protein behaved as a monomer under purification conditions. Far- and… CONTINUE READING
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