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Antithrombin
From Proteopedia
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{{STRUCTURE_1tb6| PDB=1tb6 | SIZE=400| SCENE= |right|CAPTION=Antithrombin (beige) complex with thrombin heavy chain (pink), light chain (green) and heparin polysaccharide, [[1tb6]] }} | {{STRUCTURE_1tb6| PDB=1tb6 | SIZE=400| SCENE= |right|CAPTION=Antithrombin (beige) complex with thrombin heavy chain (pink), light chain (green) and heparin polysaccharide, [[1tb6]] }} | ||
| - | '''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''' (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]]. |
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Revision as of 11:03, 29 December 2014
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.
3D structures of antithrombin
Updated on 29-December-2014
