STKE: Serpins Save Cells

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Serpins in prokaryotes.

Members of the serpin (serine proteinase inhibitor) superfamily have been identified in higher multicellular eukaryotes (plants and animals) and viruses but not in bacteria, archaea, or fungi. Thus, the ancestral serpin and the origin of the serpin inhibitory mechanism remain obscure. In this study we characterize 12 serpin-like sequences in the genomes of prokaryotic organisms, extending this ...

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Serpins: A Conformational Trap

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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Interaction of activated protein C with serpins.

The inhibition of activated protein C by six different serine protease inhibitors (serpins) that have arginine residues in the P1 position has been investigated. Micromolar concentrations of C1-inhibitor failed to inhibit the enzyme, and it was inhibited only slowly by antithrombin III with an association rate constant (kass.) of 0.15 M-1.s-1. The kass. values for the other serpins tested (prot...

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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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ژورنال

عنوان ژورنال: Science

سال: 2007

ISSN: 0036-8075,1095-9203

DOI: 10.1126/science.318.5848.173b