Allosteric block of KCa2 channels by apamin.

@article{Lamy2010AllostericBO,
  title={Allosteric block of KCa2 channels by apamin.},
  author={C{\'e}dric Lamy and Samuel J. Goodchild and Kate L. Weatherall and David E. Jane and Jean-François Li{\'e}geois and Vincent Seutin and Neil V. Marrion},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 35},
  pages={27067-77}
}
Activation of small conductance calcium-activated potassium (K(Ca)2) channels can regulate neuronal firing and synaptic plasticity. They are characterized by their high sensitivity to the bee venom toxin apamin, but the mechanism of block is not understood. For example, apamin binds to both K(Ca)2.2 and K(Ca)2.3 with the same high affinity (K(D) approximately 5 pM for both subtypes) but requires significantly higher concentrations to block functional current (IC(50) values of approximately 100… CONTINUE READING