Overlapping binding sites of structurally different antiarrhythmics flecainide and propafenone in the subunit interface of potassium channel Kv2.1.

@article{Madeja2010OverlappingBS,
  title={Overlapping binding sites of structurally different antiarrhythmics flecainide and propafenone in the subunit interface of potassium channel Kv2.1.},
  author={Michael Madeja and Wibke Steffen and Ivana Mesi{\'c} and Bojan Garic and Boris S. Zhorov},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 44},
  pages={
          33898-905
        }
}
Kv2.1 channels, which are expressed in brain, heart, pancreas, and other organs and tissues, are important targets for drug design. Flecainide and propafenone are known to block Kv2.1 channels more potently than other Kv channels. Here, we sought to explore structural determinants of this selectivity. We demonstrated that flecainide reduced the K(+) currents through Kv2.1 channels expressed in Xenopus laevis oocytes in a voltage- and time-dependent manner. By systematically exchanging various… CONTINUE READING
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