Crystal quality and inhibitor binding by aspartic proteinases; preparation of high quality crystals of mouse renin
| Autor: | B. L. Sibanda, M. Badasso, Jon B. Cooper, Chris Dealwis, S.P. Wood |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
chemistry.chemical_classification
biology Transition (genetics) Crystal chemistry Stereochemistry Peptide Condensed Matter Physics law.invention Inorganic Chemistry Enzyme Biochemistry chemistry Enzyme inhibitor law Renin–angiotensin system Materials Chemistry biology.protein Crystallization Endothiapepsin |
| Zdroj: | Journal of Crystal Growth. 122:393-399 |
| ISSN: | 0022-0248 |
| DOI: | 10.1016/0022-0248(92)90274-m |
| Popis: | Renin from mouse submandibular glands has been highly purified and co-crystallized with a synthetic nonapeptide fragment of rat angiotensionogen in which the scissile Leu-Leu bond has been modified as a hydroxyethylene mimic of the transition state. The strong diffraction from these crystals compared to the native form is discussed in relation to the behaviour of other members of the aspartic proteinase family in crystallisation. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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