NMR resonance assignments of thrombin reveal the conformational and dynamic effects of ligation.

@article{Lechtenberg2010NMRRA,
  title={NMR resonance assignments of thrombin reveal the conformational and dynamic effects of ligation.},
  author={Bernhard C Lechtenberg and Daniel J. D. Johnson and Stefan Freund and James Andrew Huntington},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2010},
  volume={107 32},
  pages={
          14087-92
        }
}
The serine protease thrombin is generated from its zymogen prothrombin at the end of the coagulation cascade. Thrombin functions as the effector enzyme of blood clotting by cleaving several procoagulant targets, but also plays a key role in attenuating the hemostatic response by activating protein C. These activities all depend on the engagement of exosites on thrombin, either through direct interaction with a substrate, as with fibrinogen, or by binding to cofactors such as thrombomodulin. How… CONTINUE READING

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