title: Structural mechanisms underlying posttranslational modification by ubiquitin-like proteins.
abstract: Covalent attachment of ubiquitin-like proteins (Ubls) is a predominant mechanism for regulating protein function in eukaryotes. Several structurally related Ubls, such as ubiquitin, SUMO, NEDD8, and ISG15, modify a vast number of proteins, altering their functions in a variety of ways. Ubl modifications can affect the target's half-life, subcellular localization, enzymatic activity, or ability to interact with protein or DNA partners. Generally, these diverse Ubls are covalently attached via their C termini to their targets by parallel, but specific, cascades involving three classes of enzymes known as E1, E2, and E3. Structures are now available for many protein complexes in E1-E2-E3 cascades, revealing a series of modular building blocks and providing mechanistic insights into their functions.
authors.affiliation: Howard Hughes Medical Institute, Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105, USA.
authors.forename: Billy T
authors.initials: BT
authors.lastname: Dye
authors.forename: Brenda A
authors.initials: BA
authors.lastname: Schulman
mesh_terms: D000818:Animals; D001703:Biophysics / Q000379:methods; D005786:Gene Expression Regulation; D006801:Humans; D008956:Models, Chemical; D008968:Molecular Conformation; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry*; D025801:Ubiquitin / Q000737:chemistry*; D044764:Ubiquitin-Activating Enzymes / Q000737:chemistry*
chemical_list: D011506:Proteins; D025801:Ubiquitin; D044764:Ubiquitin-Activating Enzymes