Tissue factor

1AHW, 1BOY, 1DAN, 1FAK, 1J9C, 1JPS, 1O5D, 1TFH, 1UJ3, 1W0Y, 1W2K, 1WQV, 1WSS, 1WTG, 1WUN, 1WV7, 1Z6J, 2A2Q, 2AEI, 2AER, 2B7D, 2B8O, 2C4F, 2CEF, 2CEH, 2CEZ, 2CFJ, 2EC9, 2F9B, 2FIR, 2FLB, 2HFT, 2PUQ, 2ZP0, 2ZWL, 2ZZU, 3ELA, 3TH2, 3TH3, 3TH4, 4IBL, 4M7L, 4Z6A, 4ZMA, 4YLQ, 2FLR215214066ENSG00000117525ENSMUSG00000028128P13726P20352NM_001993NM_001178096NM_010171NP_001171567NP_001984NP_034301Tissue factor, also called platelet tissue factor, factor III, or CD142, is a protein encoded by the F3 gene, present in subendothelial tissue and leukocytes. Its role in the clotting process is the initiation of thrombin formation from the zymogen prothrombin. Thromboplastin defines the cascade that leads to the activation of factor X—the tissue factor pathway. In doing so it has replaced the previously named extrinsic pathway in order to eliminate ambiguity.Tissue factorBlood plasma after the addition of tissue factor1ahw: A COMPLEX OF EXTRACELLULAR DOMAIN OF TISSUE FACTOR WITH AN INHIBITORY FAB (5G9)1boy: EXTRACELLULAR REGION OF HUMAN TISSUE FACTOR1dan: COMPLEX OF ACTIVE SITE INHIBITED HUMAN BLOOD COAGULATION FACTOR VIIA WITH HUMAN RECOMBINANT SOLUBLE TISSUE FACTOR1fak: HUMAN TISSUE FACTOR COMPLEXED WITH COAGULATION FACTOR VIIA INHIBITED WITH A BPTI-MUTANT1j9c: Crystal Structure of tissue factor-factor VIIa complex1jps: Crystal structure of tissue factor in complex with humanized Fab D3h441o5d: Dissecting and Designing Inhibitor Selectivity Determinants at the S1 site Using an Artificial Ala190 Protease (Ala190 uPA)1tfh: EXTRACELLULAR DOMAIN OF HUMAN TISSUE FACTOR1uj3: Crystal structure of a humanized Fab fragment of anti-tissue-factor antibody in complex with tissue factor1w0y: TF7A_3771 COMPLEX1w2k: TF7A_4380 COMPLEX1wqv: Human Factor Viia-Tissue Factor Complexed with propylsulfonamide-D-Thr-Met-p-aminobenzamidine1wss: Human Factor Viia-Tissue Factor in Complex with peprid mimetic inhibitor that has two charge groups in P2 and P41wtg: Human Factor Viia-Tissue Factor Complexed with ethylsulfonamide-D-biphenylalanine-Gln-p-aminobenzamidine1wun: Human Factor Viia-Tissue Factor Complexed with ethylsulfonamide-D-Trp-Gln-p-aminobenzamidine1wv7: Human Factor Viia-Tissue Factor Complexed with ethylsulfonamide-D-5-propoxy-Trp-Gln-p-aminobenzamidine1z6j: Crystal Structure of a ternary complex of Factor VIIa/Tissue Factor/Pyrazinone Inhibitor2a2q: Complex of Active-site Inhibited Human Coagulation Factor VIIa with Human Soluble Tissue Factor in the Presence of Ca2+, Mg2+, Na+, and Zn2+2aei: Crystal structure of a ternary complex of factor VIIa/tissue factor and 2--3,5-difluro-4--2-pyridinyl]oxy]-benzoic acid2aer: Crystal Structure of Benzamidine-Factor VIIa/Soluble Tissue Factor complex.2b7d: Factor VIIa Inhibitors: Chemical Optimization, Preclinical Pharmacokinetics, Pharmacodynamics, and Efficacy in a Baboon Thrombosis Model2b8o: Crystal Structure of Glu-Gly-Arg-Chloromethyl Ketone-Factor VIIa/Soluble Tissue Factor Complex2c4f: CRYSTAL STRUCTURE OF FACTOR VII.STF COMPLEXED WITH PD02971212f9b: Discovery of Novel Heterocyclic Factor VIIa Inhibitors2fir: Crystal structure of DFPR-VIIa/sTF2flb: Discovery of a Novel Hydroxy Pyrazole Based Factor IXa Inhibitor2flr: Novel 5-Azaindole Factor VIIa Inhibitors2hft: THE CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF HUMAN TISSUE FACTOR AT 1.7 ANGSTROMS RESOLUTION2puq: Crystal structure of active site inhibited coagulation factor VIIA in complex with soluble tissue factor Tissue factor, also called platelet tissue factor, factor III, or CD142, is a protein encoded by the F3 gene, present in subendothelial tissue and leukocytes. Its role in the clotting process is the initiation of thrombin formation from the zymogen prothrombin. Thromboplastin defines the cascade that leads to the activation of factor X—the tissue factor pathway. In doing so it has replaced the previously named extrinsic pathway in order to eliminate ambiguity. The F3 gene encodes coagulation factor III which is a cell surface glycoprotein. This factor enables cells to initiate the blood coagulation cascades, and it functions as the high-affinity receptor for the coagulation factor VII. The resulting complex provides a catalytic event that is responsible for initiation of the coagulation protease cascades by specific limited proteolysis. Unlike the other cofactors of these protease cascades, which circulate as nonfunctional precursors, this factor is a potent initiator that is fully functional when expressed on cell surfaces. There are three distinct domains of this factor: extracellular, transmembrane, and cytoplasmic. This protein is the only one in the coagulation pathway for which a congenital deficiency has not been described. In addition to the membrane-bound tissue factor, soluble form of tissue factor was also found which results from alternatively spliced tissue factor mRNA transcripts, in which exon 5 is absent and exon 4 is spliced directly to exon 6. TF is the cell surface receptor for the serine protease factor VIIa. The best known function of tissue factor is its role in blood coagulation. The complex of TF with factor VIIa catalyzes the conversion of the inactive protease factor X into the active protease factor Xa. Together with factor VIIa, tissue factor forms the tissue factor or extrinsic pathway of coagulation. This is opposed to the intrinsic (amplification) pathway which involves both activated factor IX and factor VIII. Both pathways lead to the activation of factor X (the common pathway) which combines with activated factor V in the presence of calcium and phospholipid to produce thrombin (thromboplastin activity). TF is related to a protein family known as the cytokine receptor class II family. The members of this receptor family are activated by cytokines. Cytokines are small proteins that can influence the behavior of white blood cells. Binding of VIIa to TF has also been found to start signaling processes inside the cell. The signaling function of TF/VIIa plays a role in angiogenesis and apoptosis. Pro-inflammatory and pro-angiogenic responses are activated by TF/VIIa mediated cleavage by the protease-activated receptor 2 (PAR2). EphB2 and EphA2 of the Eph tyrosine kinase receptor (RTK) family can also be cleaved by TF/VIIa. Tissue factor belongs to the cytokine receptor protein superfamily and consists of three domains: Note that one of factor VIIa's domains, GLA domain, binds in the presence of calcium to negatively charged phospholipids, and this binding greatly enhances factor VIIa binding to tissue factor.