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Related Experiment Videos

Tissue factor: molecular recognition and cofactor function

D M Martin1, C W Boys, W Ruf

  • 1Medical Research Counsil Clinical Sciences Centre, Royal Postgraduate Medical School, London, England.

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
|July 1, 1995
PubMed
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Tissue factor (TF) activates blood coagulation during inflammation. Structural and mutagenesis studies reveal distinct sites on TF that control protease activity and substrate recognition, offering insights into coagulation regulation.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Inflammation involves the coagulation cascade, initiated by tissue factor (TF) on vascular cells.
  • TF acts as a cell-surface receptor for factor VIIa, a coagulation protease.
  • TF's cofactor function is crucial for activating factor VIIa and assembling macromolecular substrates.

Purpose of the Study:

  • To elucidate the structural basis of tissue factor (TF) function in coagulation.
  • To identify specific residues involved in TF-ligand interactions and catalytic activity.
  • To develop a model for TF's role in regulating protease activity and substrate recognition.

Main Methods:

  • X-ray crystallography to determine the structure of the TF extracellular domain.

Related Experiment Videos

  • Site-directed mutagenesis to investigate the function of specific TF residues.
  • Biochemical assays to assess TF's interaction with factor VIIa and substrates.

    • Main Results:

    • The TF extracellular domain structure reveals two C2 immunoglobulin-like modules forming a 125-degree angle.
    • Mutagenesis identified key residues in both modules essential for ligand binding.
    • Distinct structural sites within TF separately control protease catalytic activity and substrate recognition.

    Conclusions:

    • A model of TF function is proposed, integrating structural and biochemical data.
    • Catalytic activity of the bound protease and substrate recognition are regulated by separate structural sites on TF.
    • Understanding TF structure-function relationships provides insights into coagulation control mechanisms.