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Figure 5
Crystal structure of the 14-3-3σ–Sirt1pS670 complex, (a) Content of the asymmetric unit showing a 14-3-3σ monomer with bound Sirt1 peptide and missing the loop Asn70–Pro79. The normal physiological 14-3-3 dimer is formed by a symmetry-related molecule (see Supplementary Fig. S1). (b) Sirt1 peptide binding site with hydrogen-bonding network. (c) OMIT (by omitting peptide atoms) electron densities of Sirt1 peptide contoured at 2σ (green) and at 4σ (magenta). (d, e) Structure superposition of Sirt1 peptide with (d) 14-3-3 binding mode 1 (PDB entry 1qjb) and (e) mode 2 (PDB entry 1qja) peptides by fitting the pSer residue using the Coot `superpose ligand' function. C-atom coloring: Sirt1 peptide, cyan; mode 1 peptide, green; mode 2 peptide, orange.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 82| Part 1| January 2026| Pages 32-40
https://doi.org/10.1107/S2053230X25010908
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