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Biol Chem. 1997 Sep;378(9):1059-63.

Mechanisms of antithrombin polymerisation and heparin activation probed by the insertion of synthetic reactive loop peptides.

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Department of Haematology, University of Cambridge, MRC Centre, UK.


Incubation of antithrombin with a series of synthetic reactive loop peptides showed that 6-mer and 7-mer peptides, P14-P9 and P14-P8 of antithrombin respectively, induced loop-sheet polymerisation and binary complex formation. These peptides are likely to anneal to the upper part of the dominant A-sheet, favouring sheet opening and allowing insertion of a second reactive loop in the lower part of the A-sheet to form polymers. The insertion of longer peptides filled the A-sheet beyond the P7 position and prevented polymerisation. Heparinised antithrombin was more resistant to polymerisation and peptide insertion, indicating that heparin induces a conformational change that closes the A-sheet and expels the reactive loop.

[Indexed for MEDLINE]

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