The isolated H4-H5 cytoplasmic loop of Na,K-ATPase overexpressed in Escherichia coli retains its ability to bind ATP.

@article{Obil1998TheIH,
  title={The isolated H4-H5 cytoplasmic loop of Na,K-ATPase overexpressed in Escherichia coli retains its ability to bind ATP.},
  author={Tom{\'a}{\vs} Ob{\vs}il and Fabienne M{\'e}rola and Anita Lewit-Bentley and Ev{\vz}en Amler},
  journal={General physiology and biophysics},
  year={1998},
  volume={17 Suppl 1},
  pages={52-5}
}
The H4-H5 loop of the alpha-subunit of mouse brain Na,K-ATPase was expressed and isolated from Escherichia coli cells. Using fluorescence analogues of ATP, this loop was shown to retain its capability to bind ATP. Isolation of a soluble H4-H5 loop with the native ATP binding site is a crucial step for detailed studies of the molecular mechanism of ATP… CONTINUE READING