Structural basis of ubiquitylation |
| |
Authors: | VanDemark Andrew P Hill Christopher P |
| |
Affiliation: | Department of Biochemistry, 20N 1900E RM 211, University of Utah, Salt Lake City 84132, USA. |
| |
Abstract: | The attachment of the small protein ubiquitin to other proteins, a process known as ubiquitylation, is a widespread form of post-translational modification that regulates numerous cellular functions in eukaryotes. Ubiquitylation is performed by complexes of E2 and E3 enzymes that are assembled and select substrates via a series of protein-protein interactions. Recent structure determinations of the ubiquitylation machinery have revealed some of the various protein-protein interfaces involved. |
| |
Keywords: | |
本文献已被 ScienceDirect PubMed 等数据库收录! |
|