Antithrombin: Difference between revisions
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<StructureSection load='3evj' size='340' side='right' caption='Glycosylated human antithrombin III complex with heparin (PDB code [[3evj]])' scene=''> | |||
<StructureSection load='3evj' size='340' side='right' caption='Glycosylated human antithrombin III complex with heparin (PDB code [[ | |||
== Function == | == Function == | ||
Revision as of 16:23, 4 November 2015
<StructureSection load='3evj' size='340' side='right' caption='Glycosylated human antithrombin III complex with heparin (PDB code 3evj)' scene=>
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 04-November-2015