The HIP2~ubiquitin conjugate forms a non-compact monomeric thioester during di-ubiquitin synthesis.
Polyubiquitination is a post-translational event used to control the degradation of damaged or unwanted proteins by modifying the target protein with a chain of ubiquitin molecules. One potential mechanism for the assembly of polyubiquitin chains involves the dimerization of an E2 conjugating enzyme...
Main Authors: | Benjamin W Cook, Kathryn R Barber, Brian H Shilton, Gary S Shaw |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2015-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC4370575?pdf=render |
Similar Items
-
An E2-ubiquitin thioester-driven approach to identify substrates modified with ubiquitin and ubiquitin-like molecules
by: Gábor Bakos, et al.
Published: (2018-11-01) -
The Ubiquitin Conjugating Enzyme: An Important Ubiquitin Transfer Platform in Ubiquitin-Proteasome System
by: Weigang Liu, et al.
Published: (2020-04-01) -
Crystal structures of an E1–E2–ubiquitin thioester mimetic reveal molecular mechanisms of transthioesterification
by: Lingmin Yuan, et al.
Published: (2021-04-01) -
Ubiquitin-Conjugating Enzymes in Cancer
by: Quyen Thu Bui, et al.
Published: (2021-06-01) -
Identification and Characterization of an E2 Ubiquitin-Conjugating Enzyme in GCM1 Ubiquitination
by: Meng-Hsiu Chiang, et al.
Published: (2008)