6F08
14-3-3 zeta in complex with the human Son of sevenless homolog 1 (SOS1)
Summary for 6F08
Entry DOI | 10.2210/pdb6f08/pdb |
Descriptor | 14-3-3 protein zeta/delta, Son of sevenless homolog 1, PENTAETHYLENE GLYCOL, ... (4 entities in total) |
Functional Keywords | 14-3-3, sos1, dimer, phosphosite, peptide binding protein |
Biological source | Homo sapiens (Human) More |
Cellular location | Cytoplasm : P63104 |
Total number of polymer chains | 8 |
Total formula weight | 111595.48 |
Authors | Ballone, A.,Centorrino, F.,Ottmann, C.,Guo, S.,Leysen, S. (deposition date: 2017-11-17, release date: 2018-02-14, Last modification date: 2024-10-09) |
Primary citation | Ballone, A.,Centorrino, F.,Wolter, M.,Ottmann, C. Structural characterization of 14-3-3 zeta in complex with the human Son of sevenless homolog 1 (SOS1). J. Struct. Biol., 202:210-215, 2018 Cited by PubMed Abstract: The deviant Ras activation machinery is found in approximately 30% of all human cancers. SOS1 is an important protagonist of this pathway that plays a key-role in aberrant cell proliferation and differentiation. Interaction of SOS1 with 14-3-3 proteins modulates SOS1 activity in Ras-MAPK signaling. In the present study, we analyze the 14-3-3/SOS1 protein-protein interaction (PPI) by different biochemical assays and report the high resolution crystal structure of a 13-mer motif of SOS1 bound to 14-3-3ζ. These structural and functional insights are important for the evaluation of this PPI interface for small-molecule stabilization as a new starting point for modulating the Ras-Raf-MAPK pathway. PubMed: 29408703DOI: 10.1016/j.jsb.2018.01.011 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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