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

• Published in: Nature (London) 1997-10, Vol.389 (6650), p.455-462
• Main Authors: Doolittle, Russell F, Spraggon, Glen, Everse, Stephen J
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Biological and medical sciences; Blood coagulation. Blood cells; Cellular biology; Cross-Linking Reagents; Crystallography, X-Ray; Fibrin - chemistry; Fibrin Fibrinogen Degradation Products - chemistry; Fundamental and applied biological sciences. Psychology; General aspects, investigation methods, hemostasis, fibrinolysis; Humanities and Social Sciences; Humans; Medical research; Models, Molecular; Molecular and cellular biology; Molecular Sequence Data; multidisciplinary; Peptide Fragments; Polymers; Protein Conformation; Proteins; Science; Science (multidisciplinary); Scientific imaging
• ISSN: 0028-0836; 1476-4687
• DOI: 10.1038/38947

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.