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Conformational flexibility in the active sites of aspartyl proteinases revealed by a pepstatin fragment binding to penicillopepsin.
Crystals of the molecular complex between the esterified tripeptide fragment of pepstatin and the aspartyl proteinase penicillopepsin are isomorphous with crystals of native penicillopepsin. The difference electron-density map at 1.8-A resolution, computed by using the amplitude differences and refi...
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| Autores principales: | , , , , |
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| Formato: | Artículo |
| Lenguaje: | en |
| Publicado: |
1982
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC347074/ https://ncbi.nlm.nih.gov/pubmed/6755464 |
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