X-ray structure of clotting factor IXa: active site and module structure related to Xase activity and hemophilia B.

@article{Hussermann1995XraySO,
  title={X-ray structure of clotting factor IXa: active site and module structure related to Xase activity and hemophilia B.},
  author={Katharina H{\"a}ussermann and Matthias R. Bauer and Robert Huber and P Lollar and Wolfram Bode},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1995},
  volume={92 21},
  pages={9796-800}
}
Hereditary deficiency of factor IXa (fIXa), a key enzyme in blood coagulation, causes hemophilia B, a severe X chromosome-linked bleeding disorder afflicting 1 in 30,000 males; clinical studies have identified nearly 500 deleterious variants. The x-ray structure of porcine fIXa described here shows the atomic origins of the disease, while the spatial distribution of mutation sites suggests a structural model for factor X activation by phospholipid-bound fIXa and cofactor VIIIa. The 3.0-A… CONTINUE READING

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