Tissue factor pathway inhibitor: Difference between revisions
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<StructureSection load='1zr0' size='450' side='right' caption='Human tissue factor pathway inhibitor 2 | <StructureSection load='1zr0' size='450' side='right' caption='Human tissue factor pathway inhibitor 2 Kunitz domain I (green) complex with trypsin (cyan) and Ca+2 ion (PDB code [[1zr0]])' scene='70/707370/Cv/1'> | ||
== Function == | == Function == | ||
'''Tissue factor pathway inhibitor''' (TFPI) is a protease inhibitor which inhibits coagulation factor Xa and VIIa<ref>PMID:9112630</ref>. 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. | '''Tissue factor pathway inhibitor''' (TFPI) is a protease inhibitor which inhibits coagulation factor Xa and VIIa<ref>PMID:9112630</ref>. 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. | ||
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The expression of hTFPI-2 in tumors is inversely related to their malignancy<ref>PMID:18000791</ref>. TFPI inhibitors are investigated as therapeutic agents agains hemophilia<ref>PMID:27207418</ref>. | The expression of hTFPI-2 in tumors is inversely related to their malignancy<ref>PMID:18000791</ref>. TFPI inhibitors are investigated as therapeutic agents agains hemophilia<ref>PMID:27207418</ref>. | ||
== Structural highlights == | == 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<ref>PMID:15932872</ref>. | In the complex of TFPI-2 and trypsin, <scene name='70/707370/Cv/2'>hydrophobic residues of TFPI-2 interact with hydrophobic patch of trypsin</scene>. An <scene name='70/707370/Cv/4'>Arg residue which is the P1 residue of TFPI-2 interacts with Asp - the S1 residue of trypsin</scene><ref>PMID:15932872</ref>. | ||
</StructureSection> | </StructureSection> | ||
Revision as of 07:50, 15 September 2016
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3D Structures of tissue factor pathway inhibitor
Updated on 15-September-2016
1adz – hTFPI-1 kunitz domain II (mutant) – human - NMR
1irh – hTFPI-1 kunitz domain III - NMR
1tfx – hTFPI-1 kunitz domain II + trypsin
1zr0 – hTFPI-2 kunitz domain I + trypsin
4dtg – hTFPI-1 kunitz domain II + antibody
4bqd – hTFPI-1 kunitz domain I + peptide
