Structural dynamics of the E6AP/UBE3A-E6-p53 enzyme-substrate complex

Structural dynamics of the E6AP/UBE3A-E6-p53 enzyme-substrate complex

Oncoprotein E6 facilitates the E6AP-catalyzed ubiquitination of p53. Here, the authors study the structural basis of this process by qualitative and quantitative cross-linking mass spectrometry, providing insights into E6AP-E6-p53 complex assembly and the conformational dynamics that enable p53 ubiq...

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Autores principales: Carolin Sailer, Fabian Offensperger, Alexandra Julier, Kai-Michael Kammer, Ryan Walker-Gray, Matthew G. Gold, Martin Scheffner, Florian Stengel
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2018
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Acceso en línea:https://doaj.org/article/665259f0303c4a7a8d8b890e1f4e21c3
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spelling oai:doaj.org-article:665259f0303c4a7a8d8b890e1f4e21c32021-12-02T17:31:31ZStructural dynamics of the E6AP/UBE3A-E6-p53 enzyme-substrate complex10.1038/s41467-018-06953-02041-1723https://doaj.org/article/665259f0303c4a7a8d8b890e1f4e21c32018-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-06953-0https://doaj.org/toc/2041-1723Oncoprotein E6 facilitates the E6AP-catalyzed ubiquitination of p53. Here, the authors study the structural basis of this process by qualitative and quantitative cross-linking mass spectrometry, providing insights into E6AP-E6-p53 complex assembly and the conformational dynamics that enable p53 ubiquitination.Carolin SailerFabian OffenspergerAlexandra JulierKai-Michael KammerRyan Walker-GrayMatthew G. GoldMartin ScheffnerFlorian StengelNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Carolin Sailer
Fabian Offensperger
Alexandra Julier
Kai-Michael Kammer
Ryan Walker-Gray
Matthew G. Gold
Martin Scheffner
Florian Stengel
Structural dynamics of the E6AP/UBE3A-E6-p53 enzyme-substrate complex
description Oncoprotein E6 facilitates the E6AP-catalyzed ubiquitination of p53. Here, the authors study the structural basis of this process by qualitative and quantitative cross-linking mass spectrometry, providing insights into E6AP-E6-p53 complex assembly and the conformational dynamics that enable p53 ubiquitination.
format article
author Carolin Sailer
Fabian Offensperger
Alexandra Julier
Kai-Michael Kammer
Ryan Walker-Gray
Matthew G. Gold
Martin Scheffner
Florian Stengel
author_facet Carolin Sailer
Fabian Offensperger
Alexandra Julier
Kai-Michael Kammer
Ryan Walker-Gray
Matthew G. Gold
Martin Scheffner
Florian Stengel
author_sort Carolin Sailer
title Structural dynamics of the E6AP/UBE3A-E6-p53 enzyme-substrate complex
title_short Structural dynamics of the E6AP/UBE3A-E6-p53 enzyme-substrate complex
title_full Structural dynamics of the E6AP/UBE3A-E6-p53 enzyme-substrate complex
title_fullStr Structural dynamics of the E6AP/UBE3A-E6-p53 enzyme-substrate complex
title_full_unstemmed Structural dynamics of the E6AP/UBE3A-E6-p53 enzyme-substrate complex
title_sort structural dynamics of the e6ap/ube3a-e6-p53 enzyme-substrate complex
publisher Nature Portfolio
publishDate 2018
url https://doaj.org/article/665259f0303c4a7a8d8b890e1f4e21c3
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