The structure of the potassium channel: molecular basis of K+ conduction and selectivity.

@article{Doyle1998TheSO,
  title={The structure of the potassium channel: molecular basis of K+ conduction and selectivity.},
  author={Declan A Doyle and J H Morais Cabral and Richard A Pfuetzner and Anling Kuo and Jacqueline M. Gulbis and Steven L. Cohen and Brian T Chait and Roderick MacKinnon},
  journal={Science},
  year={1998},
  volume={280 5360},
  pages={69-77}
}
The potassium channel from Streptomyces lividans is an integral membrane protein with sequence similarity to all known K+ channels, particularly in the pore region. X-ray analysis with data to 3.2 angstroms reveals that four identical subunits create an inverted teepee, or cone, cradling the selectivity filter of the pore in its outer end. The narrow selectivity filter is only 12 angstroms long, whereas the remainder of the pore is wider and lined with hydrophobic amino acids. A large water… CONTINUE READING
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