C

FIGURE 35.1. A 14-3-3 dimer with bound peptide ligands at the binding sites. The two C-termini (C) are indicated, as is dimerization over the N-termini, although it should be noted that the complete full-length C and N termini are not shown. 14-3-3 proteins are shown as helices, and ligands are shown as ball-and-stick models. Created from mmdbId:36278 using Cn3D.

FIGURE 35.1. A 14-3-3 dimer with bound peptide ligands at the binding sites. The two C-termini (C) are indicated, as is dimerization over the N-termini, although it should be noted that the complete full-length C and N termini are not shown. 14-3-3 proteins are shown as helices, and ligands are shown as ball-and-stick models. Created from mmdbId:36278 using Cn3D.

has often been demonstrated, but the basis for this is not easy to determine since the binding site within 14-3-3 is much conserved between isoforms and binding analysis of 14-3-3 isoforms to phosphopeptide libraries showed little discrimination. Binding specificity may depend on a number of factors including post-translational phospho-rylation of the client protein or of 14-3-3 [23], C-terminal inhibition of binding [24, 25], specific amino acid sequence variations in loop 8 of the C-terminal [26, 27], tissue-specific expression and subcellular location of both 14-3-3 and client protein [27, 28], and the steric accessibility of binding sites.

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