1FZA
CRYSTAL STRUCTURE OF FIBRINOGEN FRAGMENT D
Summary for 1FZA
| Entry DOI | 10.2210/pdb1fza/pdb |
| Descriptor | FIBRINOGEN, 2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | blood coagulation, plasma, platelet, fibrinogen, fibrin |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 6 |
| Total formula weight | 168843.04 |
| Authors | Spraggon, G.,Everse, S.J.,Doolittle, R.F. (deposition date: 1997-08-05, release date: 1997-12-03, Last modification date: 2024-11-13) |
| 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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