8ANB
14-3-3 sigma sirtuin-1 phospho-peptide complex
Summary for 8ANB
| Entry DOI | 10.2210/pdb8anb/pdb |
| Related | 1YWT |
| Descriptor | 14-3-3 protein sigma, Sirtuin 1 deacetylase, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | human sirtuin, human 14-3-3 sigma, protein complex, phospho-peptide, nad, deacetylase, peptide binding protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 27306.27 |
| Authors | Weyand, M.,Steegborn, C.,Debbert, L. (deposition date: 2022-08-05, release date: 2023-08-16, Last modification date: 2026-04-01) |
| Primary citation | Weyand, M.,Quast, L.,Steegborn, C. Potential 14-3-3 binding sites in sirtuins reveal extended phosphosite-recognition modes. Acta Crystallogr.,Sect.F, 82:32-40, 2026 Cited by PubMed Abstract: The adapter proteins of the 14-3-3 family modulate the activity and/or localization of their binding partners, which they capture if a generic target motif is in its phosphorylated state. Here, we report the identification of potential 14-3-3 binding sites in human sirtuin deacylases by bioinformatic analysis. We then characterize the interactions of peptides representing phosphorylation sites in sirtuin 3 (pS103) and sirtuin 1 (pS670) with 14-3-3 proteins. We further describe the crystal structures of complexes of 14-3-3σ with either of the two phosphopeptides. As a conclusion, we propose a more extended 14-3-3 binding mode on the N-terminal side of the phosphorylation site and the possibility of nongeneric motifs and conformations on the C-terminal side, still resulting in the known high binding affinity of the two partners. PubMed: 41410196DOI: 10.1107/S2053230X25010908 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.64 Å) |
Structure validation
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