title: Structural basis of 14-3-3 protein functions.
abstract: The 14-3-3 proteins, a family of conserved regulatory molecules, participate in a wide range of cellular processes through binding interactions with hundreds of structurally and functionally diverse proteins. Several distinct mechanisms of the 14-3-3 protein function were described, including conformational modulation of the bound protein, masking of its sequence-specific or structural features, and scaffolding that facilitates interaction between two simultaneously bound proteins. Details of these functional modes, especially from the structural point of view, still remain mostly elusive. This review gives an overview of the current knowledge concerning the structure of 14-3-3 proteins and their complexes as well as the insights it provides into the mechanisms of their functions. We discuss structural basis of target recognition by 14-3-3 proteins, common structural features of their complexes and known mechanisms of 14-3-3 protein-dependent regulations.
authors.affiliation: Department of Physical and Macromolecular Chemistry, Faculty of Science, Charles University in Prague, 12843 Prague, Czech Republic. obsil@natur.cuni.cz
authors.forename: Tomas
authors.initials: T
authors.lastname: Obsil
authors.forename: Veronika
authors.initials: V
authors.lastname: Obsilova
mesh_terms: D048948:14-3-3 Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D004268:DNA-Binding Proteins; D056890:Eukaryota / Q000378:metabolism*; D014644:Genetic Variation; D006801:Humans; D008958:Models, Molecular; D010766:Phosphorylation; D011485:Protein Binding; D011487:Protein Conformation; D054730:Protein Interaction Domains and Motifs; D020033:Protein Isoforms / Q000737:chemistry / Q000378:metabolism; D017434:Protein Structure, Tertiary
chemical_list: D048948:14-3-3 Proteins; D004268:DNA-Binding Proteins; D020033:Protein Isoforms