Probing the outer mouth structure of the HERG channel with peptide toxin footprinting and molecular modeling.

@article{Tseng2007ProbingTO,
  title={Probing the outer mouth structure of the HERG channel with peptide toxin footprinting and molecular modeling.},
  author={Gea-Ny Tseng and Kailas D. Sonawane and Yuliya V. Korolkova and Mei Zhang and Jie Liu and Eugene V. Grishin and H. Robert Guy},
  journal={Biophysical journal},
  year={2007},
  volume={92 10},
  pages={
          3524-40
        }
}
Previous studies have shown that the unusually long S5-P linker lining human ether a-go-go related gene's (hERG's) outer vestibule is critical for its channel function: point mutations at high-impact positions here can interfere with the inactivation process and, in many cases, also reduce the pore's K+ selectivity. Because no data are available on the equivalent region in the available K channel crystal structures to allow for homology modeling, we used alternative approaches to model its… CONTINUE READING

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