Crystal structure of an anticoagulant protein in complex with the Gla domain of factor X.

@article{Mizuno2001CrystalSO,
  title={Crystal structure of an anticoagulant protein in complex with the Gla domain of factor X.},
  author={Hana Mizuno and Zui Fujimoto and Hideko Atoda and Takashi Morita},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2001},
  volume={98 13},
  pages={7230-4}
}
The gamma-carboxyglutamic acid (Gla) domain of blood coagulation factors is responsible for Ca2+-dependent phospholipid membrane binding. Factor X-binding protein (X-bp), an anticoagulant protein from snake venom, specifically binds to the Gla domain of factor X. The crystal structure of X-bp in complex with the Gla domain peptide of factor X at 2.3-A resolution showed that the anticoagulation is based on the fact that two patches of the Gla domain essential for membrane binding are buried in… CONTINUE READING

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Structure 7, R277–R279

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  • 1999

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