title: Structural basis of ubiquitylation.
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.
authors.affiliation: Department of Biochemistry, 20N 1900E RM 211, University of Utah, Salt Lake City 84132, USA.
authors.forename: Andrew P
authors.initials: AP
authors.lastname: VanDemark
authors.forename: Christopher P
authors.initials: CP
authors.lastname: Hill
mesh_terms: D008025:Ligases / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D009097:Multienzyme Complexes; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D025801:Ubiquitin / Q000378:metabolism*
chemical_list: D009097:Multienzyme Complexes; D021122:Protein Subunits; D025801:Ubiquitin; D008025:Ligases