Antithrombin: Difference between revisions
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{{STRUCTURE_3evj| PDB=3evj | SIZE=400| SCENE= |right|CAPTION=Antithrombin (beige) complex with thrombin heavy chain (pink), light chain (green) and heparin polysaccharide, [[1tb6]] }} | {{STRUCTURE_3evj| PDB=3evj | SIZE=400| SCENE= |right|CAPTION=Antithrombin (beige) complex with thrombin heavy chain (pink), light chain (green) and heparin polysaccharide, [[1tb6]] }} | ||
<StructureSection load='3evj' size='340' side='right' caption='Tyrosine aminomutase complex with peptide-derived chromophore cofactor (PDB code [[2ohy]])' scene=''> | |||
'''Antithrombin''' (AT) inactivates several enzymes of the coagulation cycle. α-AT contains 4 occupied glycosylation sites and is found in blood palsma. β-AT contains only 3 occupied glycosylation sites. AT-I refers to the absorption of thrombin to fibrin; AT-II and heparin interfere with the interaction of thrombin and fibrinogen; AT-III inactivates thrombin in plasma; AT-IV becomes activated during blood coagulation. See details for the antithrombin pentasaccharide complex in [[Molecular Playground/Antithrombin-Heparin]]. | '''Antithrombin''' (AT) inactivates several enzymes of the coagulation cycle. α-AT contains 4 occupied glycosylation sites and is found in blood palsma. β-AT contains only 3 occupied glycosylation sites. AT-I refers to the absorption of thrombin to fibrin; AT-II and heparin interfere with the interaction of thrombin and fibrinogen; AT-III inactivates thrombin in plasma; AT-IV becomes activated during blood coagulation. See details for the antithrombin pentasaccharide complex in [[Molecular Playground/Antithrombin-Heparin]]. | ||
Revision as of 12:25, 3 November 2015
Template:STRUCTURE 3evj <StructureSection load='3evj' size='340' side='right' caption='Tyrosine aminomutase complex with peptide-derived chromophore cofactor (PDB code 2ohy)' scene=> Antithrombin (AT) inactivates several enzymes of the coagulation cycle. α-AT contains 4 occupied glycosylation sites and is found in blood palsma. β-AT contains only 3 occupied glycosylation sites. AT-I refers to the absorption of thrombin to fibrin; AT-II and heparin interfere with the interaction of thrombin and fibrinogen; AT-III inactivates thrombin in plasma; AT-IV becomes activated during blood coagulation. See details for the antithrombin pentasaccharide complex in Molecular Playground/Antithrombin-Heparin.
FunctionFunction
Antithrombin (AT) inactivates several enzymes of the coagulation cycle. AT is relatively inactive until it binds the heparan sidechains of the microvasculature.
▪ α-AT contains 4 occupied glycosylation sites and is found in blood palsma.
▪ β-AT contains only 3 occupied glycosylation sites.
▪ AT-I refers to the absorption of thrombin to fibrin.
▪ AT-II and heparin interfere with the interaction of thrombin and fibrinogen.
▪ AT-III inactivates thrombin in plasma.
▪ AT-IV becomes activated during blood coagulation.
See details for the antithrombin pentasaccharide complex in Molecular Playground/Antithrombin-Heparin.
DiseaseDisease
AT deficiency diseases are: Acquired AT deficiency and Inherited AT deficiency. AT deficiency is involved in thrombosis and pulmonary embolism.
RelevanceRelevance
AT activity is enhanced upon binding to the anticoagulant drug heparin.
Structural highlightsStructural highlights
The binding of AT to the heparans or the heparin drug is to a core pentasaccharide. The binding induces conformational change of AT.
3D structures of antithrombin3D structures of antithrombin
Updated on 03-November-2015