1FZB
CRYSTAL STRUCTURE OF CROSSLINKED FRAGMENT D
Summary for 1FZB
Entry DOI | 10.2210/pdb1fzb/pdb |
Descriptor | FIBRINOGEN, PEPTIDE LIGAND GPRG, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
Functional Keywords | blood coagulation, plasma, platelet, fibrinogen, fibrin |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 8 |
Total formula weight | 169696.02 |
Authors | Spraggon, G.,Everse, S.J.,Doolittle, R.F. (deposition date: 1997-08-05, release date: 1997-12-03, Last modification date: 2024-10-30) |
Primary citation | Spraggon, G.,Everse, S.J.,Doolittle, R.F. Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin. Nature, 389:455-462, 1997 Cited by 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. PubMed: 9333233DOI: 10.1038/38947 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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