Crystal structure of Mg2+- and Ca2+-bound Gla domain of factor IX complexed with binding protein.

@article{Shikamoto2003CrystalSO,
  title={Crystal structure of Mg2+- and Ca2+-bound Gla domain of factor IX complexed with binding protein.},
  author={Yasuo Shikamoto and Takashi Morita and Zui Fujimoto and Hiroshi Mizuno},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 26},
  pages={24090-4}
}
Factor IX is an indispensable protein required in the blood coagulation cascade. It binds to the surface of phospholipid membrane by means of a gamma-carboxyglutamic acid (Gla) domain situated at the N terminus. Recently, we showed that physiological concentrations of Mg2+ ions affect the native conformation of the Gla domain and in doing so augment the biological activity of factor IXa and binding affinity with its binding protein even in the presence of Ca2+ ions. Here we report on the… CONTINUE READING

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