Antithrombin: Difference between revisions
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The binding of AT to the heparans or the heparin drug is to a core pentasaccharide. The binding induces conformational change of AT. | 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 antithrombin== | |||
[[Antithrombin 3D structures]] | |||
</StructureSection> | </StructureSection> | ||
Revision as of 11:56, 18 March 2019
FunctionAntithrombin (AT) inactivates several enzymes of the coagulation cycle. AT is relatively inactive until it binds the heparan sidechains of the microvasculature.[1] ▪ α-AT contains 4 occupied glycosylation sites and is found in blood palsma. DiseaseAT deficiency diseases are: Acquired AT deficiency and Inherited AT deficiency. AT deficiency is involved in thrombosis and pulmonary embolism. RelevanceAT activity is enhanced upon . Structural highlightsThe 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 antithrombin
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3D structures of antithrombin3D structures of antithrombin
Updated on 18-March-2019
ReferencesReferences
- ↑ Li W, Johnson DJ, Esmon CT, Huntington JA. Structure of the antithrombin-thrombin-heparin ternary complex reveals the antithrombotic mechanism of heparin. Nat Struct Mol Biol. 2004 Sep;11(9):857-62. Epub 2004 Aug 15. PMID:15311269 doi:10.1038/nsmb811