An invisible ubiquitin conformation is required for efficient phosphorylation by PINK1

The Ser/Thr protein kinase PINK1 phosphorylates the well‐folded, globular protein ubiquitin (Ub) at a relatively protected site, Ser65. We previously showed that Ser65 phosphorylation results in a conformational change in which Ub adopts a dynamic equilibrium between the known, common Ub conformatio...

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Detalles Bibliográficos
Autores principales: Gladkova, Christina, Schubert, Alexander F, Wagstaff, Jane L, Pruneda, Jonathan N, Freund, Stefan MV, Komander, David
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2017
Materias:
Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5730886/
https://www.ncbi.nlm.nih.gov/pubmed/29133469
http://dx.doi.org/10.15252/embj.201797876

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5730886/
https://www.ncbi.nlm.nih.gov/pubmed/29133469
http://dx.doi.org/10.15252/embj.201797876

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