Ubiquitin‐conjugating Enzymes

Abstract

Originally published in: Protein Degradation, Volume 1. Edited by R. John Mayer, Aaron Ciechanover and Martin Rechsteiner. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30837‐8 The sections in this article are Introduction Historical Background What is an E2? Functional Diversity of Ubiquitin‐conjugating Enzymes Functions Related to Proteasome Proteolysis Endocytosis and Trafficking Non‐proteolytic Functions E2s of Uncertain Function E2 Enzymes and Disease E2 Enzymes Dedicated to Ubiquitin‐like Proteins (UbLs) The Biochemistry of E2 Enzymes E1 Interaction Interactions with Thiol‐linked Ubiquitin E3 Interactions RING E3/E2 Interactions U‐box E3/E2 Interactions HECT E3/E2 Interactions E2/Substrate Interactions E2 Catalysis Mechanism Functional Diversification of the E2 Fold Conclusions

Ubiquitin- and ubiquitin-like proteins-conjugating enzymes (E2s) in breast cancer

“…Two loops between the b-sheet and the active site and between the second and third a helix are also important in the formation of the shallow groove that surrounds the active cysteine. The active cysteine accepting ubiquitin or a UBL is found after the fourth b-sheet strand and immediately amino-terminal to the small 3 10 helix in a shallow groove constructed, in addition to these two structures, by residues from the third and fourth a helices [12] (Fig. 1b).…”