Antithrombin: Difference between revisions

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== Relevance ==
== Relevance ==
AT activity is enhanced upon <scene name='46/466527/Cv/2'>binding to the anticoagulant drug heparin</scene>.
AT activity is enhanced upon <scene name='46/466527/Cv/3'>binding to the anticoagulant drug heparin</scene>.


==Structural highlights==
==Structural highlights==

Revision as of 12:23, 8 December 2015


Function

Antithrombin (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.
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.

Disease

AT deficiency diseases are: Acquired AT deficiency and Inherited AT deficiency. AT deficiency is involved in thrombosis and pulmonary embolism.

Relevance

AT activity is enhanced upon .

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.

Glycosylated human antithrombin III complex with heparin (in green) (PDB code 3evj)

Drag the structure with the mouse to rotate

3D structures of antithrombin3D structures of antithrombin

Updated on 08-December-2015

ReferencesReferences

  1. 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky