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© Structural Dynamics Of Macromolecules
The structure of a bacterial analog of the nicotinic receptor (one color per subunit) inserted into the cell membrane (grey and orange). A representation of the volume accessible to ions is shown in yellow.
Publication : Biochimie

Antithrombin III: structural and functional aspects.

Team: Architecture and Dynamics of Biological Macromolecules
Member: Marc Delarue
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Biochimie - 01 Aug 1990

Mourey L, Samama JP, Delarue M, Choay J, Lormeau JC, Petitou M, Moras D.

Link to Pubmed [PMID] – 2126464

Link to DOI – 10.1016/0300-9084(90)90123-x

Biochimie. 1990 Aug;72(8):599-608. Review.

Antithrombin III is a plasma glycoprotein responsible for thrombin inhibition in the blood coagulation cascade. The X-ray structure of its cleaved form has been determined and refined to 3.2 A resolution. The overall topology is similar to that of alpha 1-antitrypsin, another member of the serpin (serine protease inhibitor) superfamily. The biological activity of antithrombin III is mediated by a polysaccharide, heparin. The binding site of this effector is described. A possible structural transition from the native to the cleaved structure is discussed.