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Article

Allosteric activation of antithrombin critically depends upon hinge region extension.

The Journal of biological chemistry - 5 Nov 2004

Langdown Jonathan, Johnson Daniel J D, Baglin Trevor P, Huntington James A

Abstract excerpt

Antithrombin (AT) inhibits most of the serine proteases generated in the blood coagulation cascade, but its principal targets are factors IXa, Xa, and thrombin. Heparin binding to AT, via a specific pentasaccharide sequence, alters the conformation of AT in a way that promotes efficient inhibition of factors IXa and Xa, but not of thrombin. The conformational change most likely to be relevant to protease...

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Identifiers

PMID: 15326167
DOI: 10.1074/jbc.M408961200

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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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Allosteric activation of antithrombin critically depends upon hinge region extension.PMID 15326167Read ↗

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