Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin
| Autor: | Russell F. Doolittle, G. Spraggon, Stephen J. Everse |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
Models
Molecular Protein Conformation Stereochemistry Dimer Molecular Sequence Data Crystallography X-Ray Fibrinogen Fibrin Fibrin Fibrinogen Degradation Products chemistry.chemical_compound Protein structure medicine Humans Molecular replacement Amino Acid Sequence Peptide sequence Multidisciplinary biology Peptide Fragments Cross-Linking Reagents chemistry Coagulation Covalent bond biology.protein medicine.drug |
| Zdroj: | Nature. 389:455-462 |
| ISSN: | 1476-4687 0028-0836 |
| DOI: | 10.1038/38947 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|