Antithrombin: Difference between revisions
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▪ '''AT-I''' refers to the absorption of thrombin to fibrin.<br /> | ▪ '''AT-I''' refers to the absorption of thrombin to fibrin.<br /> | ||
▪ '''AT-II''' and heparin interfere with the interaction of thrombin and fibrinogen.<br /> | ▪ '''AT-II''' and heparin interfere with the interaction of thrombin and fibrinogen.<br /> | ||
▪ '''AT-III''' inactivates thrombin in plasma.<br /> | ▪ '''AT-III''' inactivates thrombin in plasma. For details see [[Student Projects for UMass Chemistry 423 Spring 2012-7|Student Projects for UMass Chemistry 423 Spring 2012-7 - Antithrombin III: Devourer of Memories]].<br /> | ||
▪ '''AT-IV''' becomes activated during blood coagulation.<br /> | ▪ '''AT-IV''' becomes activated during blood coagulation.<br /> | ||
See details for the antithrombin pentasaccharide complex in [[Molecular Playground/Antithrombin-Heparin]]. | See details for the antithrombin pentasaccharide complex in [[Molecular Playground/Antithrombin-Heparin]]. | ||
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== Relevance == | == Relevance == | ||
AT activity is enhanced upon <scene name='46/466527/Cv/ | AT activity is enhanced upon <scene name='46/466527/Cv/4'>binding to the anticoagulant drug heparin</scene>. | ||
==Structural highlights== | ==Structural highlights== | ||
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== | ==3D structures of antithrombin== | ||
[[Antithrombin 3D structures]] | |||
</StructureSection> | |||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Latest revision as of 12:58, 25 December 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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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