Molecular basis for Kv1.5 channel block: conservation of drug binding sites among voltage-gated K+ channels.

@article{Decher2004MolecularBF,
  title={Molecular basis for Kv1.5 channel block: conservation of drug binding sites among voltage-gated K+ channels.},
  author={Niels Decher and Bernard Pirard and Florian Bundis and Stefan Peukert and Karl-Heinz Baringhaus and A. E. Busch and Klaus Steinmeyer and Michael C Sanguinetti},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 1},
  pages={394-400}
}
Kv1.5 channels conduct the ultrarapid delayed rectifier current (IKur) that contributes to action potential repolarization of human atrial myocytes. Block of these channels has been proposed as a treatment for atrial arrhythmias. Here we report a novel and potent inhibitor of Kv1.5 potassium channels, N-benzyl-N-pyridin-3-yl-methyl-2-(toluene-4-sulfonylamino)-benzamide hydrochloride (S0100176), which exhibits features consistent with preferential block of the open state. The IC50 of S0100176… CONTINUE READING