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Entropic stabilization of a deubiquitinase provides conformational plasticity and slow unfolding kinetics beneficial for functioning on the proteasome
Human ubiquitin C-terminal hydrolyase UCH-L5 is a topologically knotted deubiquitinase that is activated upon binding to the proteasome subunit Rpn13. The length of its intrinsically disordered cross-over loop is essential for substrate recognition. Here, we showed that the catalytic domain of UCH-L...
Tallennettuna:
| Julkaisussa: | Sci Rep |
|---|---|
| Päätekijät: | , , , , , |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
Nature Publishing Group
2017
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5364529/ https://ncbi.nlm.nih.gov/pubmed/28338014 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/srep45174 |
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