Mechanism of Block of Single Protopores of the Torpedo Chloride Channel Clc-0 by 2-(p-Chlorophenoxybutyric) Acid (Cpb)

@article{Pusch2001MechanismOB,
  title={Mechanism of Block of Single Protopores of the Torpedo Chloride Channel Clc-0 by 2-(p-Chlorophenoxybutyric) Acid (Cpb)},
  author={Michael Pusch and Alessio Accardi and Antonella Liantonio and Loretta Ferrera and Annamaria De Luca and Diana Conte Camerino and Franco Conti},
  journal={The Journal of General Physiology},
  year={2001},
  volume={118},
  pages={45 - 62}
}
We investigated in detail the mechanism of inhibition by the S(-) enantiomer of 2-(p-chlorophenoxy)butyric acid (CPB) of the Torpedo Cl(-)channel, ClC-0. The substance has been previously shown to inhibit the homologous skeletal muscle channel, CLC-1. ClC-0 is a homodimer with probably two independently gated protopores that are conductive only if an additional common gate is open. As a simplification, we used a mutant of ClC-0 (C212S) that has the common gate "locked open" (Lin, Y.W., C.W. Lin… CONTINUE READING
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