Antithrombin III: structural and functional aspects.

L Mourey; J P Samama; M Delarue; J Choay; J C Lormeau; M Petitou; D Moras

doi:10.1016/0300-9084(90)90123-x

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Antithrombin III: structural and functional aspects.

L Mourey·J P Samama·M Delarue·J Choay·J C Lormeau·M Petitou·D Moras

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Abstract

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.

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Amino Acid Sequence Animals Antithrombin III Carbohydrates Humans Molecular Sequence Data Protein Conformation Structure-Activity Relationship X-Ray Diffraction alpha 1-Antitrypsin Journal Article Research Support, Non-U.S. Gov't Review

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L Mourey, J P Samama, M Delarue, J Choay, J C Lormeau, M Petitou, D Moras. 1990. Antithrombin III: structural and functional aspects.. https://doi.org/10.1016/0300-9084(90)90123-x

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