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Article

Conformational conversion of antithrombin to a fully activated substrate of factor Xa without need for heparin.

Biochemistry - 10 Mar 1998

Huntington J A, Gettins P G

Abstract excerpt

Regulation of the inhibitory activity of antithrombin, the principal inhibitor of the blood-clotting proteinases factor Xa and thrombin, is accomplished by binding to heparin. We report here an antithrombin variant in which serine at position 380, 14 residues N-terminal from the reactive bond and at a hinge point in the structure, was replaced by cysteine to test a proposed mechanism of heparin activation of...

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Identifiers

PMID: 9521646
DOI: 10.1021/bi972182o

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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.

Related research

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Conformational conversion of antithrombin to a fully activated substrate of factor Xa without need for heparin.PMID 9521646Read ↗

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

The use of prothrombin(S525C) labeled with fluorescein to directly study the inhibition of prothrombinase by antithrombin during prothrombin activation.Semantic proximity Read ↗

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

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

The allosteric mechanism of activation of antithrombin as an inhibitor of factor IXa and factor Xa: heparin-independent full activation through mutations adjacent to helix D.Semantic proximity Read ↗

Structure of prothrombin in the closed form reveals new details on the mechanism of activation.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 ↗

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 ↗

Conformational changes in serpins: II. The mechanism of activation of antithrombin by heparin.Semantic proximity Read ↗

Antithrombin 'DREUX' (Lys 114Glu): a variant with complete loss of heparin affinity.Semantic proximity Read ↗

Factor Xa is highly protected from antithrombin-fondaparinux and antithrombin-enoxaparin when incorporated into the prothrombinase complex.Semantic proximity Read ↗

Restricted active site docking by enzyme-bound substrate enforces the ordered cleavage of prothrombin by prothrombinase.Semantic proximity Read ↗

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