NMR spectroscopy of 14-3-3ζ reveals a flexible C-terminal extension: differentiation of the chaperone and phosphoserine-binding activities of 14-3-3ζ

Williams, Danielle M.Ecroyd, HeathGoodwin, KatyDai, HuanqinFu, HaianWoodcock, Joanna M.Zhang, LixinCarver, John2015-12-100264-6021http://hdl.handle.net/1885/63355Intracellular 14-3-3 proteins bind to many proteins, via a specific phosphoserine motif, regulating diverse cellular tasks including cell signalling and disease progression. The 14-3-3ζ isoform is a molecular chaperone, preventing the stressinduced aggreKeywords: chaperone; phosphoserine; small heat shock protein; stratifin; amino acid sequence; article; binding affinity; carboxy terminal sequence; controlled study; genetic conservation; ligand binding; nonhuman; nuclear magnetic resonance spectroscopy; priority j 14-3-3 protein; Biophysical characterization; C-terminal flexibility; Molecular chaperone; Protein aggregation; Protein-protein interactionNMR spectroscopy of 14-3-3ζ reveals a flexible C-terminal extension: differentiation of the chaperone and phosphoserine-binding activities of 14-3-3ζ201110.1042/BJ201021782016-02-24