Antithrombin activity of a peptide corresponding to residues 54-75 of heparin cofactor II.

@article{Hortin1989AntithrombinAO,
  title={Antithrombin activity of a peptide corresponding to residues 54-75 of heparin cofactor II.},
  author={Glen L. Hortin and Douglas M. Tollefsen and Barbara M. Benutto},
  journal={The Journal of biological chemistry},
  year={1989},
  volume={264 24},
  pages={
          13979-82
        }
}
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51 Citations

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The complete N-terminal extension of heparin cofactor II is required for maximal effectiveness as a thrombin exosite 1 ligand
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The results support a model in which thrombin first binds to GAGs, followed by HCII addition to the ternary complex and release of HCII 1-75 for exosite 1 binding and serpin mechanism inhibition.
Glycosaminoglycan-binding properties and kinetic characterization of human heparin cofactor II expressed in Escherichia coli.
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The thrombin-bound structure of the peptide fragment, hirudin 55-65, has been determined by use of transferred NOE spectroscopy and the apparent preference for a gauche- (chi 1 = +60) side-chain conformation of Ile(59) in the bound state may be explained by the existence of a positively charged arginine residue among the hydrophobic residues in theThrombin exosite.
Deciphering the structural elements of hirudin C-terminal peptide that bind to the fibrinogen recognition site of alpha-thrombin.
  • J. Chang
  • Biology, Chemistry
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  • 1991
TLDR
The anticoagulant activities of hirudin C-terminal peptides were quantitatively related to their abilities to shield the five identified lysines of thrombin.
Evidence for multiple enzyme site involvement in the modulation of thrombin activity by products of prothrombin proteolysis.
Alpha-thrombin-catalyzed hydrolysis of fibrin I. Alternative binding modes and the accessibility of the active site in fibrin I-bound alpha-thrombin.
The reaction of thrombin with platelet-derived nexin requires a secondary recognition site in addition to the catalytic site.
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