6twz

14-3-3 sigma complexed with a phosphorylated 16E6 peptide

spinqualitylabelsall models 6twz, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: B3P, TAR, TPO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Protein-protein interaction motifs are often alterable by post-translational modifications. For example, 19% of predicted human PDZ domain-binding motifs (PBMs) have been experimentally proven to be phosphorylated, and up to 82% are theoretically phosphorylatable. Phosphorylation of PBMs may drastically rewire their interactomes, by altering their affinities for PDZ domains and 14-3-3 proteins. The effect of phosphorylation is often analyzed by performing "phosphomimetic" mutations. Here, we focused on the PBMs of HPV16-E6 viral oncoprotein and human RSK1 kinase. We measured the binding affinities of native, phosphorylated, and phosphomimetic variants of both PBMs toward the 266 human PDZ domains. We co-crystallized all the motif variants with a selected PDZ domain to characterize the structural consequence of the different modifications. Finally, we elucidated the structural basis of PBM capture by 14-3-3 proteins. This study provides novel atomic and interactomic insights into phosphorylatable dual specificity motifs and the differential effects of phosphorylation and phosphomimetic approaches. Dual Specificity PDZ- and 14-3-3-Binding Motifs: A Structural and Interactomics Study.,Gogl G, Jane P, Caillet-Saguy C, Kostmann C, Bich G, Cousido-Siah A, Nyitray L, Vincentelli R, Wolff N, Nomine Y, Sluchanko NN, Trave G Structure. 2020 Apr 6. pii: S0969-2126(20)30092-7. doi:, 10.1016/j.str.2020.03.010. PMID:32294469 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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