An NMR study of the N-terminal domain of wild-type hERG and a T65P trafficking deficient hERG mutant.

@article{Gayen2011AnNS,
  title={An NMR study of the N-terminal domain of wild-type hERG and a T65P trafficking deficient hERG mutant.},
  author={Shovanlal Gayen and Qingxin Li and Angela Shuyi Chen and Thị Th{\'u}y Hạnh Nguyễn and Qiwei Huang and Jeffrey Hill and Congbao Kang},
  journal={Proteins},
  year={2011},
  volume={79 8},
  pages={
          2557-65
        }
}
The human Ether-à-go-go Related Gene (hERG) potassium channel plays an important role in the heart by controlling the rapid delayed rectifier current. The N-terminal 135 residues (NTD) contain a Per-Arnt-Sim (PAS) domain and an N-terminal amphipathic helix. NMR relaxation analysis and H/D exchange experiments on the NTD demonstrated that the amphipathic helix is rigid and solvent accessible. An NTD containing a T65P mutation, which causes a hERG channel trafficking deficiency, was purified from… CONTINUE READING
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