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The structural basis for 14-3-3:phosphopeptide binding specificity.

Cell | Dec 26, 1997

http://www.ncbi.nlm.nih.gov/pubmed/9428519

The 14-3-3 family of proteins mediates signal transduction by binding to phosphoserine-containing proteins. Using phosphoserine-oriented peptide libraries to probe all mammalian and yeast 14-3-3s, we identified two different binding motifs, RSXpSXP and RXY/FXpSXP, present in nearly all known 14-3-3 binding proteins. The crystal structure of 14-3-3zeta complexed with the phosphoserine motif in polyoma middle-T was determined to 2.6 A resolution. The bound peptide is in an extended conformation, with a tight turn created by the pS +2 Pro in a cis conformation. Sites of peptide-protein interaction in the complex rationalize the peptide library results. Finally, we show that the 14-3-3 dimer binds tightly to single molecules containing tandem repeats of phosphoserine motifs, implicating bidentate association as a signaling mechanism with molecules such as Raf, BAD, and Cbl.

Pubmed ID: 9428519 RIS Download

Mesh terms: 14-3-3 Proteins | Crystallography, X-Ray | Enzyme Inhibitors | Humans | Models, Molecular | Molecular Sequence Data | Peptide Library | Phosphopeptides | Phosphorylation | Phosphoserine | Protein Binding | Protein Conformation | Proteins | Substrate Specificity | Tyrosine 3-Monooxygenase

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Associated grants

  • Agency: NIGMS NIH HHS, Id: GM56203
  • Agency: NIGMS NIH HHS, Id: R01 GM056203

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