Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin

Glen Spraggon, Stephen J. Everse and Russell F. Doolittle ()
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Russell F. Doolittle: Center for Molecular Genetics, University of California

Nature, 1997, vol. 389, issue 6650, 455-462

Abstract: 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 Å resolution. The 86K three-chained structure consists of a coiled-coil region and two homologous globular entities 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.

Date: 1997
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DOI: 10.1038/38947

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