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. 2010 Aug 21;66(Pt 9):978–984. doi: 10.1107/S1744309110025479

Figure 1.

Figure 1

Structure of the 14-3-3σ–YAP pS127 peptide complex. (a) Cartoon representation of the 14-3-3σ dimer (red and dark red) in complex with the YAP pS127 peptide (yellow and light yellow; stick representation). The binding pocket created by helices 3, 5, 7 and 9 and the dimerization site are clearly visible, as well as the orientation of the peptide in the binding pocket. (b) Electrostatic interactions (dotted lines) of the phosphorylated residue pSer127 of the YAP pS127 peptide (yellow; stick representation) in the binding groove and residues Lys49, Arg56, Arg129 and Tyr130 of the 14-3-3 protein (red; cartoon representation). The backbone of the peptide is further coordinated by residues Asn42, Lys122, Asn175, Asp225 and Asn226 of the 14-3-3 protein. (c) A 2F o − F c electron-density map for the YAP pS127 peptide (yellow, stick representation) is shown in white. Water molecules are indicated as light blue balls. The density map is contoured at 1σ. (d) Stereo image of the binding pocket. Colouring is as in (b).