Antithrombin III: structural and functional aspects

L. Mourey (1) , J.P. P Samama (1) , M. Delarue (1) , J. Choay (1) , J.C. Lormeau , M. Petitou , D. Moras

1 IBMC - Institut de biologie moléculaire et cellulaire

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

Domains: Life Sciences [q-bio]

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