Osteopontin binds multiple calcium ions with high affinity and independently of phosphorylation status.

@article{Klning2014OsteopontinBM,
  title={Osteopontin binds multiple calcium ions with high affinity and independently of phosphorylation status.},
  author={Eva Kl{\"a}ning and Brian Christensen and Esben Skipper S\orensen and Thomas Vorup-Jensen and Jan K Jensen},
  journal={Bone},
  year={2014},
  volume={66},
  pages={90-5}
}
Osteopontin (OPN) is an acidic, intrinsically disordered extracellular matrix protein with a capacity to modulate biomineralization in vitro and in vivo. The role of posttranslational modification of osteopontin has been intensively studied. Phosphorylation of OPN has been demonstrated to play a role in inhibition of biomineral formation and growth in vitro. Here, we used isothermal titration calorimetry (ITC) to investigate the ability of OPN to bind the divalent cations Ca(2+) and Mg(2… CONTINUE READING

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