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Article

Conformational activation of antithrombin by heparin involves an altered exosite interaction with protease.

The Journal of biological chemistry - 5 Dec 2014

Izaguirre Gonzalo, Aguila Sonia, Qi Lixin, Swanson Richard, Roth Ryan, Rezaie Alireza R, Gettins Peter G W, Olson Steven T

Abstract excerpt

Heparin allosterically activates antithrombin as an inhibitor of factors Xa and IXa by enhancing the initial Michaelis complex interaction of inhibitor with protease through exosites. Here, we investigate the mechanism of this enhancement by analyzing the effects of alanine mutations of six putative antithrombin exosite residues and three complementary protease exosite residues on antithrombin reactivity with...

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Identifiers

PMID: 25331949
DOI: 10.1074/jbc.M114.611707
PMCID: PMC4256340

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Conformational activation of antithrombin by heparin involves an altered exosite interaction with protease.PMID 25331949Read ↗

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 ↗

Allosteric activation of antithrombin critically depends upon hinge region extension.Semantic proximity Read ↗

Paramount Importance of Core Conformational Changes for Heparin Allosteric Activation of Antithrombin.Semantic proximity Read ↗

The elusive role of the potential factor X cation-binding exosite-1 in substrate and inhibitor interactions.Semantic proximity Read ↗

Selective disruption of heparin and antithrombin-mediated regulation of human factor IX.Semantic proximity Read ↗

The signature 3-O-sulfo group of the anticoagulant heparin sequence is critical for heparin binding to antithrombin but is not required for allosteric activation.Semantic proximity Read ↗

Inhibition of a thrombin anion-binding exosite-2 mutant by the glycosaminoglycan-dependent serpins protein C inhibitor and heparin cofactor II.Semantic proximity Read ↗

An RNA aptamer exploits exosite-dependent allostery to achieve specific inhibition of coagulation factor IXaSemantic proximity Read ↗

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

Proexosite-1 on prothrombin is a factor Va-dependent recognition site for the prothrombinase complex.Semantic proximity Read ↗

The heparin-binding exosite of factor IXa is a critical regulator of plasma thrombin generation and venous thrombosis.Semantic proximity Read ↗

Saturation Mutagenesis of the Antithrombin Reactive Center Loop P14 Residue Supports a Three-step Mechanism of Heparin Allosteric Activation Involving Intermediate and Fully Activated States.Semantic proximity Read ↗

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