The second Kunitz domain of human tissue factor pathway inhibitor: cloning, structure determination and interaction with factor Xa.

@article{Burgering1997TheSK,
  title={The second Kunitz domain of human tissue factor pathway inhibitor: cloning, structure determination and interaction with factor Xa.},
  author={Maurits J. M. Burgering and L P Orbons and A van der Doelen and John W. M. Mulders and Henri J. M. Theunissen and Peter D. J. Grootenhuis and Wolfram Bode and Robert Huber and Milton T Stubbs},
  journal={Journal of molecular biology},
  year={1997},
  volume={269 3},
  pages={395-407}
}
Tissue Factor Pathway Inhibitor (TFPI) is a 36 kDa glycoprotein that helps maintain haemostasis by inhibiting Factor Xa and the Factor VIIa/Tissue Factor (TF) complex. TFPI contains three tandemly linked Kunitz inhibitor domains, of which the second inhibits factor Xa. We have undertaken a multidisciplinary approach to study the structure and function of the second Kunitz domain of TFPI, with a view towards the rational design of factor Xa inhibitors. Amino acid residues 93 to 154 of the mature… CONTINUE READING
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