Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d)
| Autor: | Edgar F. Meyer, F.X. Gomis-Ruth, Istvan Botos, Wolfram Bode, Dachuan Zhang, F. G. Njoroge, C. Blood, R. Doll, J. W. Fox |
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| Rok vydání: | 1994 |
| Předmět: |
Models
Molecular Stereochemistry Molecular Sequence Data Venom Biology Matrix metalloproteinase Crystallography X-Ray chemistry.chemical_compound Crotalid Venoms Amino Acid Sequence Binding site Peptide sequence Metalloproteinase Crotalus atrox Binding Sites Multidisciplinary Metalloendopeptidases biology.organism_classification Amides Protein Structure Tertiary Zinc Biochemistry chemistry Tyrosine Pyroglutamic acid Research Article Atrolysin C |
| Zdroj: | Proceedings of the National Academy of Sciences. 91:8447-8451 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.91.18.8447 |
| Popis: | The structure of the metalloproteinase and hemorrhagic toxin atrolysin C form d (EC 3.4.24.42), from the venom of the western diamondback rattlesnake Crotalus atrox, has been determined to atomic resolution by x-ray crystallographic methods. This study illuminates the nature of inhibitor binding with natural (< Glu-Asn-Trp, where < Glu is pyroglutamic acid) and synthetic (SCH 47890) ligands. The primary specificity pocket is exceptionally deep; the nature of inhibitor and productive substrate binding is discussed. Insights gained from the study of these complexes facilitate the design of potential drugs to treat diseases where matrix metalloproteinases have been implicated, e.g., arthritis and tumor metastasis. |
| Databáze: | OpenAIRE |
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