Voltage-dependent and -independent titration of specific residues accounts for complex gating of a ClC chloride channel by extracellular protons.

@article{Niemeyer2009VoltagedependentA,
  title={Voltage-dependent and -independent titration of specific residues accounts for complex gating of a ClC chloride channel by extracellular protons.},
  author={Mar{\'i}a Isabel Niemeyer and L. Pablo Cid and Yamil R Yusef and Rodolfo Briones and Francisco V Sep{\'u}lveda},
  journal={The Journal of physiology},
  year={2009},
  volume={587 Pt 7},
  pages={1387-400}
}
The ClC transport protein family comprises both Cl(-) ion channel and H(+)/Cl(-) and H(+)/NO(3)(-) exchanger members. Structural studies on a bacterial ClC transporter reveal a pore obstructed at its external opening by a glutamate side-chain which acts as a gate for Cl(-) passage and in addition serves as a staging post for H(+) exchange. This same conserved glutamate acts as a gate to regulate Cl(-) flow in ClC channels. The activity of ClC-2, a genuine Cl(-) channel, has a biphasic response… CONTINUE READING

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