Bouvignies Guillaume, Blackledge Martin
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).
Chembiochem. 2015 May 4;16(7):1033-4. doi: 10.1002/cbic.201500101. Epub 2015 Mar 20.
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.
核磁共振光谱法和等温滴定量热法最近被结合起来，以证明内在无序的真核翻译起始因子4E结合蛋白2（4E-BP2）的磷酸化如何诱导其折叠成稳定的三维结构。经典的结构-功能范式被颠倒了，磷酸化诱导的折叠抑制了与真核翻译起始因子4E（eIF4E）的结合，从而有助于调节这种相互作用。
