Skip to Main content Skip to Navigation
Journal articles

Antithrombin III: structural and functional aspects

Abstract : Antithrombin Ill is a plasma glycoprotein responsib!e 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 6,rantitrypsin, anothe ~. member of the serpin (serine protease inhibitor) superfamily. The biological activity of antithrombin III is mediated by a polysaccharide, heparir. The binding site of this effector is described. A possible structural transition from the native to the cleaved structure is discussed. antithrombin !I1 / X.ray structure / heparin / serpin superfamily
Document type :
Journal articles
Complete list of metadata
Contributor : Lionel Mourey Connect in order to contact the contributor
Submitted on : Friday, November 20, 2020 - 4:54:35 PM
Last modification on : Monday, June 21, 2021 - 7:36:02 PM


Publisher files allowed on an open archive




L. Mourey, J.P. P Samama, M. Delarue, J. Choay, J.C. Lormeau, et al.. Antithrombin III: structural and functional aspects. Biochimie, Elsevier, 1990, 72 (8), pp.599-608. ⟨10.1016/0300-9084(90)90123-x⟩. ⟨hal-03004833⟩



Record views


Files downloads