response to vitamin K / coagulation factor Xa / platelet alpha granule / Cargo concentration in the ER / Defective factor IX causes thrombophilia / Defective cofactor function of FVIIIa variant / Defective F9 variant does not activate FX / blood circulation / Extrinsic Pathway of Fibrin Clot Formation / COPII-mediated vesicle transport ...response to vitamin K / coagulation factor Xa / platelet alpha granule / Cargo concentration in the ER / Defective factor IX causes thrombophilia / Defective cofactor function of FVIIIa variant / Defective F9 variant does not activate FX / blood circulation / Extrinsic Pathway of Fibrin Clot Formation / COPII-mediated vesicle transport / positive regulation of lipid kinase activity / positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway / COPII-coated ER to Golgi transport vesicle / cytolysis by host of symbiont cells / thrombospondin receptor activity / Defective factor XII causes hereditary angioedema / thrombin / regulation of blood coagulation / neutrophil-mediated killing of gram-negative bacterium / ligand-gated ion channel signaling pathway / Defective F8 cleavage by thrombin / Platelet Aggregation (Plug Formation) / negative regulation of astrocyte differentiation / negative regulation of platelet activation / positive regulation of collagen biosynthetic process / negative regulation of cytokine production involved in inflammatory response / positive regulation of TOR signaling / positive regulation of blood coagulation / negative regulation of fibrinolysis / Gamma-carboxylation of protein precursors / Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus / Common Pathway of Fibrin Clot Formation / Removal of aminoterminal propeptides from gamma-carboxylated proteins / regulation of cytosolic calcium ion concentration / fibrinolysis / Intrinsic Pathway of Fibrin Clot Formation / endoplasmic reticulum-Golgi intermediate compartment membrane / Peptide ligand-binding receptors / positive regulation of release of sequestered calcium ion into cytosol / platelet alpha granule lumen / acute-phase response / Regulation of Complement cascade / negative regulation of proteolysis / Cell surface interactions at the vascular wall / lipopolysaccharide binding / Post-translational protein phosphorylation / positive regulation of receptor signaling pathway via JAK-STAT / growth factor activity / positive regulation of insulin secretion / phospholipid binding / platelet activation / response to wounding / positive regulation of protein localization to nucleus / Golgi lumen / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / positive regulation of reactive oxygen species metabolic process / antimicrobial humoral immune response mediated by antimicrobial peptide / blood coagulation / extracellular vesicle / Thrombin signalling through proteinase activated receptors (PARs) / Platelet degranulation / heparin binding / positive regulation of cell growth / regulation of cell shape / G alpha (q) signalling events / collagen-containing extracellular matrix / blood microparticle / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / cell surface receptor signaling pathway / positive regulation of cell migration / positive regulation of protein phosphorylation / G protein-coupled receptor signaling pathway / copper ion binding / endoplasmic reticulum lumen / external side of plasma membrane / serine-type endopeptidase activity / signaling receptor binding / positive regulation of cell population proliferation / calcium ion binding / proteolysis / extracellular space / extracellular exosome / extracellular region / membrane / plasma membrane Similarity search - Function
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)
HL049413
United States
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)
HL139554
United States
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)
HL147821
United States
Childrens Discovery Institute of Washington University and St. Louis Childrens Hospital
CDI-CORE-2015-505
United States
Childrens Discovery Institute of Washington University and St. Louis Childrens Hospital
CDI-CORE-2019-813
United States
Foundation for Barnes-Jewish Hospital
3770
United States
Other private
Washington University Diabetes Research Center DK020579
Other private
The Alvin J. Siteman Cancer Center at Barnes-Jewish Hospital and Washington University School of Medicine CA091842
Citation
Journal: Subcell Biochem / Year: 2024 Title: The Prothrombin-Prothrombinase Interaction. Authors: Bosko M Stojanovski / Bassem M Mohammed / Enrico Di Cera / Abstract: The hemostatic response to vascular injury entails a sequence of proteolytic events where several inactive zymogens of the trypsin family are converted to active proteases. The cascade starts with ...The hemostatic response to vascular injury entails a sequence of proteolytic events where several inactive zymogens of the trypsin family are converted to active proteases. The cascade starts with exposure of tissue factor from the damaged endothelium and culminates with conversion of prothrombin to thrombin in a reaction catalyzed by the prothrombinase complex composed of the enzyme factor Xa, cofactor Va, Ca, and phospholipids. This cofactor-dependent activation is paradigmatic of analogous reactions of the blood coagulation and complement cascades, which makes elucidation of its molecular mechanism of broad significance to the large class of trypsin-like zymogens to which prothrombin belongs. Because of its relevance as the most important reaction in the physiological response to vascular injury, as well as the main trigger of pathological thrombotic complications, the mechanism of prothrombin activation has been studied extensively. However, a molecular interpretation of this mechanism has become available only recently from important developments in structural biology. Here we review current knowledge on the prothrombin-prothrombinase interaction and outline future directions for the study of this key reaction of the coagulation cascade.
Entire : Prothrombin_Prothrombinase complex on lipid nanodiscs.
Entire
Name: Prothrombin_Prothrombinase complex on lipid nanodiscs.
Components
Complex: Prothrombin_Prothrombinase complex on lipid nanodiscs.
Organelle or cellular component: Coagulation Factor Va
Organelle or cellular component: Coagulation Factor Xa
Organelle or cellular component: Prothrombin
-
Supramolecule #1: Prothrombin_Prothrombinase complex on lipid nanodiscs.
Supramolecule
Name: Prothrombin_Prothrombinase complex on lipid nanodiscs. type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 Details: The complex is made of coagulation factor Va (derived from human plasma), coagulation factor Xa (Recombinantly expressed in BHK cells) and Prothrombin (Recombinantly expressed in BHK cells). ...Details: The complex is made of coagulation factor Va (derived from human plasma), coagulation factor Xa (Recombinantly expressed in BHK cells) and Prothrombin (Recombinantly expressed in BHK cells). The nanodisc component of the complex is made of the scaffold protein MSP1E3D1 (Recombinantly expressed in bacteria) and the phospholipid component was Porcine Brain phosphatidylserine.
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