Blocker protection in the pore of a voltage-gated K+ channel and its structural implications

@article{Camino2000BlockerPI,
  title={Blocker protection in the pore of a voltage-gated K+ channel and its structural implications},
  author={Donato del Camino and Miguel Holmgren and Yi Liu and Gary Yellen},
  journal={Nature},
  year={2000},
  volume={403},
  pages={321-325}
}
The structure of the bacterial potassium channel KcsA has provided a framework for understanding the related voltage-gated potassium channels (Kv channels) that are used for signalling in neurons. Opening and closing of these Kv channels (gating) occurs at the intracellular entrance to the pore, and this is also the site at which many open channel blockers affect Kv channels. To learn more about the sites of blocker binding and about the structure of the open Kv channel, we investigated here… CONTINUE READING

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