Different Fast-Gate Regulation by External Cl− and H+ of the Muscle-Type Clc Chloride Channels

@article{Chen2001DifferentFR,
  title={Different Fast-Gate Regulation by External Cl− and H+ of the Muscle-Type Clc Chloride Channels},
  author={Mei-fang Chen and T Chen},
  journal={The Journal of General Physiology},
  year={2001},
  volume={118},
  pages={23 - 32}
}
The fast gate of the muscle-type ClC channels (ClC-0 and ClC-1) opens in response to the change of membrane potential (V). This gating process is intimately associated with the binding of external Cl(-) to the channel pore in a way that the occupancy of Cl(-) on the binding site increases the channel's open probability (P(o)). External H(+) also enhances the fast-gate opening in these channels, prompting a hypothesis that protonation of the binding site may increase the Cl(-) binding affinity… CONTINUE READING

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