3UAL
Crystal Structure of 14-3-3 epsilon with Mlf1 peptide
Summary for 3UAL
| Entry DOI | 10.2210/pdb3ual/pdb |
| Related | 2BR9 3UBW |
| Descriptor | 14-3-3 protein epsilon, Myeloid leukemia factor 1, TERTIARY-BUTYL ALCOHOL, ... (4 entities in total) |
| Functional Keywords | adapter protein, all helical, phosphopetide, signaling protein-protein binding complex, signaling protein/protein binding |
| Biological source | Homo sapiens (human) More |
| Cellular location | Nucleus : P62258 Cytoplasm : P58340 |
| Total number of polymer chains | 2 |
| Total formula weight | 28589.63 |
| Authors | Weyand, M.,Ottmann, C. (deposition date: 2011-10-21, release date: 2012-01-25, Last modification date: 2024-11-27) |
| Primary citation | Molzan, M.,Weyand, M.,Rose, R.,Ottmann, C. Structural insights of the MLF1/14-3-3 interaction. Febs J., 279:563-571, 2012 Cited by PubMed Abstract: Myeloid leukaemia factor 1 (MLF1) binds to 14-3-3 adapter proteins by a sequence surrounding Ser34 with the functional consequences of this interaction largely unknown. We present here the high-resolution crystal structure of this binding motif [MLF1(29-42)pSer34] in complex with 14-3-3ε and analyse the interaction with isothermal titration calorimetry. Fragment-based ligand discovery employing crystals of the binary 14-3-3ε/MLF1(29-42)pSer34 complex was used to identify a molecule that binds to the interface rim of the two proteins, potentially representing the starting point for the development of a small molecule that stabilizes the MLF1/14-3-3 protein-protein interaction. Such a compound might be used as a chemical biology tool to further analyse the 14-3-3/MLF1 interaction without the use of genetic methods. Database Structural data are available in the Protein Data Bank under the accession number(s) 3UAL [14-3-3ε/MLF1(29-42)pSer34 complex] and 3UBW [14-3-3ε/MLF1(29-42)pSer34/3-pyrrolidinol complex] Structured digital abstract • 14-3-3 epsilon and MLF1 bind by x-ray crystallography (View interaction) • 14-3-3 epsilon and MLF1 bind by isothermal titration calorimetry (View Interaction: 1, 2). PubMed: 22151054DOI: 10.1111/j.1742-4658.2011.08445.x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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