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The ternary complex of antithrombin–anhydrothrombin–heparin reveals the basis of inhibitor specifici...

The ternary complex of antithrombin–anhydrothrombin–heparin reveals the basis of inhibitor specifici...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_228342966

The ternary complex of antithrombin–anhydrothrombin–heparin reveals the basis of inhibitor specificity

About this item

Full title

The ternary complex of antithrombin–anhydrothrombin–heparin reveals the basis of inhibitor specificity

Publisher

New York: Nature Publishing Group US

Journal title

Nature structural & molecular biology, 2004-09, Vol.11 (9), p.863-867

Language

English

Formats

Publication information

Publisher

New York: Nature Publishing Group US

More information

Scope and Contents

Contents

Antithrombin, the principal physiological inhibitor of the blood coagulation proteinase thrombin, requires heparin as a cofactor. We report the crystal structure of the rate-determining encounter complex formed between antithrombin, anhydrothrombin and an optimal synthetic 16-mer oligosaccharide. The antithrombin reactive center loop projects from...

Alternative Titles

Full title

The ternary complex of antithrombin–anhydrothrombin–heparin reveals the basis of inhibitor specificity

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_journals_228342966

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_228342966

Other Identifiers

ISSN

1545-9993

E-ISSN

1545-9985

DOI

10.1038/nsmb810

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