Crystal structure of the native plasminogen reveals an activation-resistant compact conformation.

@article{Xue2012CrystalSO,
  title={Crystal structure of the native plasminogen reveals an activation-resistant compact conformation.},
  author={Yafeng Xue and Cristian Bodin and K Olsson},
  journal={Journal of thrombosis and haemostasis : JTH},
  year={2012},
  volume={10 7},
  pages={1385-96}
}
BACKGROUND Plasminogen is the zymogen form of plasmin and the precursor of angiostatin. It has been implicated in a variety of disease states, including thrombosis, bleeding and cancers. The native plasminogen, known as Glu-plasminogen, contains seven domains comprising the N-terminal peptide domain (NTP), five kringle domains (K1-K5) and the C-terminal serine protease domain (SP). Previous studies have established that the lysine binding site (LBS) of the conserved kringle domains plays a… CONTINUE READING

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