Figure 4
Figure 4. Structure of the 14-3-3ζ/phospho-β2 complex. (A) Overall structure of the 14-3-3ζ dimer and 2 peptides. The protein is shown as a surface representation colored according to surface charge as implemented in PyMOL. (B) The difference electron density map (Fo − Fc) of the β2 phosphopeptide calculated from the final model without the peptide, shown at σ = 2. The α-helices E and H of 14-3-3 are located below and above the peptide, respectively, and shown as a ribbon diagram. (C) Same as panel B, but the final model of the peptide is also shown. (D) The same as panel C, but shown from above.

Structure of the 14-3-3ζ/phospho-β2 complex. (A) Overall structure of the 14-3-3ζ dimer and 2 peptides. The protein is shown as a surface representation colored according to surface charge as implemented in PyMOL. (B) The difference electron density map (Fo − Fc) of the β2 phosphopeptide calculated from the final model without the peptide, shown at σ = 2. The α-helices E and H of 14-3-3 are located below and above the peptide, respectively, and shown as a ribbon diagram. (C) Same as panel B, but the final model of the peptide is also shown. (D) The same as panel C, but shown from above.

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