کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2185702 | 1096003 | 2011 | 6 صفحه PDF | دانلود رایگان |

14-3-3 proteins participate in many key cellular processes after binding to disordered phospho-partners. Usually, the phosphorylated state is an essential target for the binding. Here, we show for the first time residues other than those in the 14-3-3 binding motif that are essential for the binding between 14-3-3 and a phosphorylated partner. Results support that phosphorylation, although necessary, is not sufficient for 14-3-3′s complex formation, as structurally constrained anchor residues play a critical function in stabilizing the protein–protein interaction.
Graphical AbstractFigure optionsDownload high-quality image (114 K)Download as PowerPoint slideResearch Highlights
► Anchor residues in a globular region of intrinsically disordered protein were determined by molecular dynamics.
► Anchor residues are essential in the interaction to 14-3-3 proteins.
► In vitro and in vivo gain or loss of function of anchor residues was demonstrated.
Journal: Journal of Molecular Biology - Volume 406, Issue 4, 4 March 2011, Pages 552–557