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...

Descripción completa

Guardado en:
Detalles Bibliográficos
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
Materias:
Science
Q
Acceso en línea:https://doaj.org/article/665259f0303c4a7a8d8b890e1f4e21c3
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!

Ejemplares similares

Ejemplares similares