Vitamin K-dependent blood coagulation proteins form hetero-dimers
| Autor: | C. W. G. Boys, M. P. Esnouf, Colin C.F. Blake, S. K. Holland, Karl Harlos, A. I. Burgess |
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| Rok vydání: | 1987 |
| Předmět: |
Models
Molecular Vitamin chemistry.chemical_classification Vitamin K Multidisciplinary Macromolecular Substances Protein Conformation Fibrinolysis Factor X Thrombin chemistry.chemical_element Vitamin k Calcium Blood proteins Blood Coagulation Factors chemistry.chemical_compound Enzyme Coagulation Biochemistry chemistry Humans Prothrombin Binding site Blood Coagulation |
| Zdroj: | Nature. 330:82-84 |
| ISSN: | 1476-4687 0028-0836 |
| Popis: | The later stages of the blood coagulation cascade are characterized by the presence of vitamin K-dependent proteins and their involvement in membrane-bound, multi-protein converting complexes with an essential requirement for calcium ions. Specific interactions between zymogens and activating enzymes have not yet been identified. Here we describe a crystallographic study of prothrombin fragment 1 (residues 1-156 of prothrombin) which indicates that vitamin K-dependent coagulation proteins have specific association sites that allow them to form hetero-dimers. The calcium-induced formation of a hetero-dimer between fragment 1 and factor X is demonstrated by cross-linking. Such hetero-dimers of vitamin K-dependent proteins could be significant in the coagulation system. |
| Databáze: | OpenAIRE |
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