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...

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Detalles Bibliográficos
Autores principales: Lee, Yun-Tzai Cloud, Chang, Chia-Yun, Chen, Szu-Yu, Pan, Yun-Ru, Ho, Meng-Ru, Hsu, Shang-Te Danny
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2017
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5364529/
https://www.ncbi.nlm.nih.gov/pubmed/28338014
http://dx.doi.org/10.1038/srep45174

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5364529/
https://www.ncbi.nlm.nih.gov/pubmed/28338014
http://dx.doi.org/10.1038/srep45174

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