1tb6
From Proteopedia
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'''2.5A Crystal Structure of the Antithrombin-Thrombin-Heparin Ternary Complex''' | '''2.5A Crystal Structure of the Antithrombin-Thrombin-Heparin Ternary Complex''' | ||
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[[Category: Johnson, D J.]] | [[Category: Johnson, D J.]] | ||
[[Category: Li, W.]] | [[Category: Li, W.]] | ||
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Revision as of 06:45, 3 May 2008
2.5A Crystal Structure of the Antithrombin-Thrombin-Heparin Ternary Complex
Contents |
Overview
The maintenance of normal blood flow depends completely on the inhibition of thrombin by antithrombin, a member of the serpin family. Antithrombin circulates at a high concentration, but only becomes capable of efficient thrombin inhibition on interaction with heparin or related glycosaminoglycans. The anticoagulant properties of therapeutic heparin are mediated by its interaction with antithrombin, although the structural basis for this interaction is unclear. Here we present the crystal structure at a resolution of 2.5 A of the ternary complex between antithrombin, thrombin and a heparin mimetic (SR123781). The structure reveals a template mechanism with antithrombin and thrombin bound to the same heparin chain. A notably close contact interface, comprised of extensive active site and exosite interactions, explains, in molecular detail, the basis of the antithrombotic properties of therapeutic heparin.
Disease
Known disease associated with this structure: Dysprothrombinemia OMIM:[176930], Hyperprothrombinemia OMIM:[176930], Hypoprothrombinemia OMIM:[176930]
About this Structure
1TB6 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the antithrombin-thrombin-heparin ternary complex reveals the antithrombotic mechanism of heparin., Li W, Johnson DJ, Esmon CT, Huntington JA, Nat Struct Mol Biol. 2004 Sep;11(9):857-62. Epub 2004 Aug 15. PMID:15311269 Page seeded by OCA on Sat May 3 09:45:31 2008