Conformational Changes in Thrombin When Complexed by Serpins
نویسندگان
چکیده
منابع مشابه
Thrombin inhibition by serpins disrupts exosite II.
Thrombin uses three principal sites, the active site, exosite I, and exosite II, for recognition of its many cofactors and substrates. It is synthesized in the zymogen form, prothrombin, and its activation at the end of the blood coagulation cascade results in the formation of the active site and exosite I and the exposure of exosite II. The physiological inhibitors of thrombin are all serpins,...
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Fig. 1. Representative crystal structures of members of the serpin family. Cartoon diagrams were produced using MOLSCRIPT (21): A. bovine trypsin proteinase inhibitor, pdb accession 1BPI B. cleaved antitrypsin, 7API C. inact ovalbumin, 1OVA D. inact antitrypsin, 1QLP E. docking complex between inactive trypsin and serpin 1K, 1I99 F. covalent complex between trypsin and antitrypsin, 1EZX G. late...
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Serpins are key actors of systems involving proteolytic reactions, such as the haemostatic system, as they are irreversible suicide inhibitors of serine proteases. The structural flexibility and physical properties of serpins that are required for their efficient inhibitory mechanism also make them especially vulnerable to even minor factors that induce conformational changes in the native form...
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A difference in recognition of the adhesive glycoprotein vitronectin (also called S-protein, serum spreading factor, and epibolin) by monoclonal antibody 8E6 (Hayman EG, et al, Proc Natl Acad Sci USA 80:4003, 1983) was investigated using a competitive enzyme-immunosorbent assay and immunoaffinity chromatography. Recognition of vitronectin in serum was approximately 50-fold greater than recognit...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2001
ISSN: 0021-9258
DOI: 10.1074/jbc.m108710200