title: 14-3-3 proteins: structure resolved, functions less clear.
abstract: The crystal structures of 14-3-3 proteins reveal that they form dimers with a deep groove running along the length of the dimer. The location of conserved residues in this groove suggests that it plays an essential role in the adaptor functions of these proteins.
authors.affiliation: CRC Centre for Cell and Molecular Biology, Institute of Cancer Research, London, UK.
authors.forename: R
authors.initials: R
authors.lastname: Marais
authors.forename: C
authors.initials: C
authors.lastname: Marshall
mesh_terms: D048948:14-3-3 Proteins; D000595:Amino Acid Sequence; D000818:Animals; D017124:Conserved Sequence; D046911:Macromolecular Substances; D008322:Mammals; D008958:Models, Molecular; D010751:Phosphopyruvate Hydratase / Q000737:chemistry; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D014446:Tyrosine 3-Monooxygenase
chemical_list: D048948:14-3-3 Proteins; D046911:Macromolecular Substances; D011506:Proteins; D014446:Tyrosine 3-Monooxygenase; D010751:Phosphopyruvate Hydratase