Allosteric regulation of E2:E3 interactions promote a processive ubiquitination machine

RING finger proteins constitute the large majority of ubiquitin ligases (E3s) and function by interacting with ubiquitin-conjugating enzymes (E2s) charged with ubiquitin. How low-affinity RING–E2 interactions result in highly processive substrate ubiquitination is largely unknown. The RING E3, gp78,...

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Autores principales: Das, Ranabir, Liang, Yu-He, Mariano, Jennifer, Li, Jess, Huang, Tao, King, Aaren, Tarasov, Sergey G, Weissman, Allan M, Ji, Xinhua, Byrd, R Andrew
Formato: Artigo
Lenguaje:Inglês
Publicado: European Molecular Biology Organization 2013
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Article
Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC3770950/
https://ncbi.nlm.nih.gov/pubmed/23942235
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/emboj.2013.174
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