2c23
14-3-3 PROTEIN BETA (HUMAN) IN COMPLEX WITH EXOENZYME S PEPTIDE
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OverviewOverview
The seven members of the human 14-3-3 protein family regulate a diverse, range of cell signaling pathways by formation of protein-protein complexes, with signaling proteins that contain phosphorylated Ser/Thr residues, within specific sequence motifs. Previously, crystal structures of three, 14-3-3 isoforms (zeta, sigma, and tau) have been reported, with structural, data for two isoforms deposited in the Protein Data Bank (zeta and sigma)., In this study, we provide structural detail for five 14-3-3 isoforms bound, to ligands, providing structural coverage for all isoforms of a human, protein family. A comparative structural analysis of the seven 14-3-3, proteins revealed specificity determinants for binding of phosphopeptides, in a specific orientation, target domain interaction surfaces and flexible, adaptation of 14-3-3 proteins through domain movements. Specifically, the, structures of the beta isoform in its apo and peptide bound forms showed, that its binding site can exhibit structural flexibility to facilitate, binding of its protein and peptide partners. In addition, the complex of, 14-3-3 beta with the exoenzyme S peptide displayed a secondary structural, element in the 14-3-3 peptide binding groove. These results show that the, 14-3-3 proteins are adaptable structures in which internal flexibility is, likely to facilitate recognition and binding of their interaction, partners.
About this StructureAbout this Structure
2C23 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for protein-protein interactions in the 14-3-3 protein family., Yang X, Lee WH, Sobott F, Papagrigoriou E, Robinson CV, Grossmann JG, Sundstrom M, Doyle DA, Elkins JM, Proc Natl Acad Sci U S A. 2006 Nov 14;103(46):17237-42. Epub 2006 Nov 3. PMID:17085597
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