Structure of the antithrombin–thrombin–heparin ternary complex reveals the antithrombotic mechanism of heparin

@article{Li2004StructureOT,
  title={Structure of the antithrombin–thrombin–heparin ternary complex reveals the antithrombotic mechanism of heparin},
  author={Wei Li and Daniel J. D. Johnson and Charles T. Esmon and James A. Huntington},
  journal={Nature Structural \&Molecular Biology},
  year={2004},
  volume={11},
  pages={857-862}
}
The maintenance of normal blood flow depends completely on the inhibition of thrombin by antithrombin, a member of the serpin family. Antithrombin circulates at a high concentration, but only becomes capable of efficient thrombin inhibition on interaction with heparin or related glycosaminoglycans. The anticoagulant properties of therapeutic heparin are mediated by its interaction with antithrombin, although the structural basis for this interaction is unclear. Here we present the crystal… Expand
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