Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin.
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Spraggon G, Everse SJ, Doolittle RF
Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin.
Nature. 1997 Oct 2;389(6650):455-62.
- PubMed ID
- 9333233 [ View in PubMed]
- Abstract
In blood coagulation, units of the protein fibrinogen pack together to form a fibrin clot, but a crystal structure for fibrinogen is needed to understand how this is achieved. The structure of a core fragment (fragment D) from human fibrinogen has now been determined to 2.9 A resolution. The 86K three-chained structure consists of a coiled-coil region and two homologous globular entitles oriented at approximately 130 degrees to each other. Additionally, the covalently bound dimer of fragment D, known as 'double-D', was isolated from human fibrin, crystallized in the presence of a Gly-Pro-Arg-Pro-amide peptide ligand, which simulates the donor polymerization site, and its structure solved by molecular replacement with the model of fragment D.