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Article

Canonical inhibitor-like interactions explain reactivity of alpha1-proteinase inhibitor Pittsburgh and antithrombin with proteinases.

The Journal of biological chemistry - 26 Sept 2003

Dementiev Alexey, Simonovic Miljan, Volz Karl, Gettins Peter G W

Abstract excerpt

The serpin antithrombin is a slow thrombin inhibitor that requires heparin to enhance its reaction rate. In contrast, alpha1-proteinase inhibitor (alpha1PI) Pittsburgh (P1 Met --> Arg natural variant) inhibits thrombin 17 times faster than pentasaccharide heparin-activated antithrombin. We present here x-ray structures of free and S195A trypsin-bound alpha1PI Pittsburgh, which show that the reactive center loop...

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Identifiers

PMID: 12860985
DOI: 10.1074/jbc.M305195200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Canonical inhibitor-like interactions explain reactivity of alpha1-proteinase inhibitor Pittsburgh and antithrombin with proteinases.PMID 12860985Read ↗

Kinetic characterization of the proteinase binding defect in a reactive site variant of the serpin, antithrombin. Role of the P1' residue in transition-state stabilization of antithrombin-proteinase complex formation.Semantic proximity Read ↗

The M358R variant of α(1)-proteinase inhibitor inhibits coagulation factor VIIa.Semantic proximity Read ↗

Heparin-activated antithrombin interacts with the autolysis loop of target coagulation proteases.Semantic proximity Read ↗

Inhibitory conformation of the reactive loop of alpha 1-antitrypsin.Semantic proximity Read ↗

Residues Tyr253 and Glu255 in strand 3 of beta-sheet C of antithrombin are key determinants of an exosite made accessible by heparin activation to promote rapid inhibition of factors Xa and IXa.Semantic proximity Read ↗

α1 -antitrypsin Pittsburgh and plasmin-mediated proteolysis.Semantic proximity Read ↗

Conformational activation of antithrombin by heparin involves an altered exosite interaction with protease.Semantic proximity Read ↗

Substitution of arginine for Leu444 in the reactive site of heparin cofactor II enhances the rate of thrombin inhibition.Semantic proximity Read ↗

P1 and P2' site mutations convert protease nexin-2 from a factor XIa inhibitor to a plasmin inhibitor.Semantic proximity Read ↗

Serine 380 (P14) --> glutamate mutation activates antithrombin as an inhibitor of factor Xa.Semantic proximity Read ↗

C1 inhibitor serpin domain structure reveals the likely mechanism of heparin potentiation and conformational disease.Semantic proximity Read ↗

Crystal structure of monomeric native antithrombin reveals a novel reactive center loop conformation.Semantic proximity Read ↗

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