Hanatoxin Modifies the Gating of a Voltage-Dependent K+ Channel through Multiple Binding Sites

@article{Swartz1997HanatoxinMT,
  title={Hanatoxin Modifies the Gating of a Voltage-Dependent K+ Channel through Multiple Binding Sites},
  author={Kenton Jon Swartz and Roderick MacKinnon},
  journal={Neuron},
  year={1997},
  volume={18},
  pages={665-673}
}
We studied the mechanism by which Hanatoxin (HaTx) inhibits the drk1 voltage-gated K+ channel. HaTx inhibits the K+ channel by shifting channel opening to more depolarized voltages. Channels opened by strong depolarization in the presence of HaTx deactivate much faster upon repolarization, indicating that toxin bound channels can open. Thus, HaTx inhibits the drk1 K+ channel, not by physically occluding the ion conduction pore, but by modifying channel gating. Occupancy of the channel by HaTx… 

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