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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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Bibliografiske detaljer
Main Authors: Kervinen, J, Tobin, G J, Costa, J, Waugh, D S, Wlodawer, A, Zdanov, A
Format: Artigo
Sprog:Inglês
Udgivet: 1999
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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