Figure 3
From: Chimeric 14-3-3 proteins for unraveling interactions with intrinsically disordered partners
Crystal structures of the pCH1 chimeric protein. (A) – molecular packing in the pCH1℧ crystal form with the phosphopeptide (red sphere) swap between monomers of two 14-3-3 dimers. 14-3-3 subunits are shown as colored ribbons forming an inverted Ω shape; one physiological 14-3-3 dimer is highlighted by a semitransparent surface. (B) – magnified view showing the linker and the phosphopeptide with the corresponding 2Fo-Fc electron density contoured at 1σ (residues are labeled, with numbers indicating positions with respect to pSer). (C) – Comparison of phosphopeptide conformations in the pCH1 (this work) and 5LU1 (synthetic HSPB6 phosphopeptide co-crystallized with 14-3-3σ27) structures. (D) – molecular packing in the pCH1X crystal form with no peptide swap (dashed lines correspond to unresolved parts of the linker).
