The single pore residue Asp542 determines Ca2+ permeation and Mg2+ block of the epithelial Ca2+ channel.

@article{Nilius2001TheSP,
  title={The single pore residue Asp542 determines Ca2+ permeation and Mg2+ block of the epithelial Ca2+ channel.},
  author={Bernd Nilius and Rudi Vennekens and Jean Prenen and Joost G. J. Hoenderop and Guy Droogmans and Ren{\'e} J M Bindels},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 2},
  pages={1020-5}
}
The epithelial Ca(2+) channel (ECaC), which was recently cloned from rabbit kidney, exhibits distinctive properties that support a facilitating role in transcellular Ca(2+) (re)absorption. ECaC is structurally related to the family of six transmembrane-spanning ion channels with a pore-forming region between S5 and S6. Using point mutants of the conserved negatively charged amino acids present in the putative pore, we have identified a single aspartate residue that determines Ca(2+) permeation… CONTINUE READING

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