Tissue factor pathway inhibitor

spinqualitylabelsall models Human tissue factor pathway inhibitor 2 Kunitz domain I (green) complex with trypsin (cyan) and Ca+2 ion (PDB code 1zr0) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Tissue factor pathway inhibitor (TFPI) is a protease inhibitor which inhibits coagulation factor Xa and VIIa. TFPI contains three Kunitz domains. The Kunitz domain is disulfide-rich and is arranged to form a twisted two-stranded antiparallel β sheet followed by an α helix. Kunitz I and II domains inhibit VIIa coagulation factor while Kunitz II domain inhibits Xa. Kunitz III domains probably involved in the interactions with lipoproteins. Relevance The expression of hTFPI-2 in tumors is inversely related to their malignancy. TFPI inhibitors are investigated as therapeutic agents agains hemophilia. Structural highlights In the complex of TFPI-2 and trypsin, hydrophobic residues of TFPI-2 interact with hydrophobic patch of trypsin. An Arg residue which is the P1 residue of TFPI-2 interacts with Asp - the S1 residue of trypsin. Ca coordination site. Water molecules are shown as red spheres.

3D Structures of tissue factor pathway inhibitor

Updated on 25-April-2022

Tissue factor pathway inhibitor domains: kunitz I 29-118; kunitz II 121-178; kunitz III 210-270

1adz – hTFPI-1 kunitz domain II (mutant) – human - NMR
1irh – hTFPI-1 kunitz domain III - NMR
1tfx – hTFPI-1 kunitz domain II + trypsin
6bx8 – hTFPI-1 kunitz domain I (mutant) + trypsin
1zr0 – hTFPI-2 kunitz domain I + trypsin
5nmv – hTFPI-1 kunitz domain I + antibody
4dtg – hTFPI-1 kunitz domain II + antibody
4bqd – hTFPI-1 kunitz domain I + peptide
7v1n – hTFPI-1 + toxin B

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