Evidence that Ser775 in the alpha subunit of the Na,K-ATPase is a residue in the cation binding pocket.

@article{Blostein1997EvidenceTS,
  title={Evidence that Ser775 in the alpha subunit of the Na,K-ATPase is a residue in the cation binding pocket.},
  author={Rhoda Blostein and Anna Wilczyńska and Steven J D Karlish and Jos{\'e} M Arg{\"u}ello and Jerry B. Lingrel},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 40},
  pages={24987-93}
}
Substitution of alanine for Ser775 in a ouabain-resistant alpha1 sheep isoform causes a 30-fold decrease in apparent affinity for K+ as an activator of the Na,K-ATPase, as well as an increase in apparent affinity for ATP (Arguello, J. M., and Lingrel, J. B (1995) J. Biol. Chem. 270, 22764-22771). This study was carried out to determine whether Ser775 is a direct cation-ligating residue or whether the change in apparent affinity for K+ is secondary to a conformational alteration as evidenced in… CONTINUE READING

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