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Structural dynamics of the E6AP/UBE3A-E6-p53 enzyme-substrate complex
oleh: Carolin Sailer, Fabian Offensperger, Alexandra Julier, Kai-Michael Kammer, Ryan Walker-Gray, Matthew G. Gold, Martin Scheffner, Florian Stengel
Format: | Article |
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Diterbitkan: | Nature Portfolio 2018-10-01 |
Deskripsi
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.