Crystallographic Evidence That the F2 Kringle Catalytic Domain Linker of Prothrombin Does Not Cover the Fibrinogen Recognition Exosite
| Autor: | Margit Bauer, Wolfram Bode, Andreas van de Locht, Milton T. Stubbs |
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| Rok vydání: | 1996 |
| Předmět: |
Models
Molecular Serine Proteinase Inhibitors Stereochemistry Molecular Sequence Data Crystal structure Crystallography X-Ray Fibrinogen Biochemistry Protein Structure Secondary Catalysis Kringles medicine Animals Humans Amino Acid Sequence Amino acid residue Rhodnius prolixus Molecular Biology Binding Sites Sequence Homology Amino Acid biology Chemistry Active site A protein Cell Biology biology.organism_classification Crystallography Insect Hormones Vertebrates biology.protein Insect Proteins Cattle Prothrombin Linker medicine.drug |
| Zdroj: | Journal of Biological Chemistry. 271:3413-3416 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.271.7.3413 |
| Popis: | The 2.6-A x-ray crystal structure of bovine α-thrombin in complex with rhodniin, a protein inhibitor isolated from the bug Rhodnius prolixus, has been solved and refined. The structure has enabled us to trace the N-terminal part of the 49-residue A-chain of bovine α-thrombin for the first time, which is fixed in a U-shaped loop on the molecular surface opposite the active site canyon. Model building shows that the 25 amino acid residues that link the A-chain and F2 kringle cannot run through the fibrinogen recognition exosite. This demonstrates that this fibrinogen recognition exosite is available in prothrombin and meizothrombin. |
| Databáze: | OpenAIRE |
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