title: Antithrombin III: structural and functional aspects.
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.
authors: Laboratoire de Cristallographie Biologique, IBMC du CNRS, Strasbourg, France.
authors: L
authors: L
authors: Mourey
authors: J P
authors: JP
authors: Samama
authors: M
authors: M
authors: Delarue
authors: J
authors: J
authors: Choay
authors: J C
authors: JC
authors: Lormeau
authors: M
authors: M
authors: Petitou
authors: D
authors: D
authors: Moras
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000990:Antithrombin III / Q000737:chemistry*; D002241:Carbohydrates / Q000737:chemistry; D006801:Humans; D008969:Molecular Sequence Data; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D014961:X-Ray Diffraction; D000515:alpha 1-Antitrypsin / Q000737:chemistry
chemical_list: D002241:Carbohydrates; D000515:alpha 1-Antitrypsin; D000990:Antithrombin III