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Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting.
We determined at 2.3 A resolution the crystal structure of prophytepsin, a zymogen of a barley vacuolar aspartic proteinase. In addition to the classical pepsin-like bilobal main body of phytepsin, we also traced most of the propeptide, as well as an independent plant-specific domain, never before d...
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| Main Authors: | , , , , , |
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| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
1999
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1171470/ https://ncbi.nlm.nih.gov/pubmed/10406799 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/18.14.3947 |
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