title: Structural biology turned on its head.
abstract: NMR spectroscopy and ITC have recently been combined to demonstrate how phosphorylation of the intrinsically disordered eukaryotic translation initiation factor 4E-binding protein 2 (4E-BP2) induces folding into a stable three-dimensional structure. The classical structure-function paradigm is inverted, with phosphorylation-induced folding inhibiting binding to the eukaryotic translation initiation factor 4E (eIF4E) and thereby contributing to regulation of the interaction.
authors: Université Grenoble Alpes, Institut de Biologie Structurale (IBS), 71 Avenue des Martyrs, 38027 Grenoble (France); CEA, DSV, IBS, 71 Avenue des Martyrs, 38027 Grenoble (France); CNRS, IBS, 71 Avenue des Martyrs, 38027 Grenoble (France).
authors: Guillaume
authors: G
authors: Bouvignies
authors: Martin
authors: M
authors: Blackledge
mesh_terms: D002151:Calorimetry; D039561:Eukaryotic Initiation Factor-4E / Q000737:chemistry* / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D010766:Phosphorylation; D017433:Protein Structure, Secondary
chemical_list: D039561:Eukaryotic Initiation Factor-4E
keywords: NMR spectroscopy; intrinsically disordered proteins; phosphorylation; protein folding