Xenbase Image ID: 136411

FIGURE 1:. Crystal structure of human Survivin with the N-terminal tail of histone H3 phosphorylated on T3. (A) Two orientations of Survivin rotated 90° relative to each other. Survivin is shown in green, and its surface is marked in gray. The peptide molecule is represented with red sticks. Insets show interactions between H3T3ph and Survivin. Inset shows the hydrogen bond network. H3T3ph carbon, nitrogen, oxygen, and phosphorus atoms are shown in dark red, blue, light red, and orange, respectively. Survivin carbon, nitrogen, and oxygen atoms of peptide-binding residues are shown as green, blue, and light red sticks, respectively. Water molecules are presented as light red spheres. Dashes depict probable hydrogen bonds. Marked residues are important in peptide binding. (B) Electrostatic potential on the Survivin surface near the peptide-binding groove. Negatively charged amino acids are marked in red, positively charged ones in blue. (C) Hydrophobicity level of binding pocket for H3T3ph mapped on the Survivin surface. Progressive color change from green to red indicates changes in amino acid hydrophobicity from hydrophilic (arginine [Arg]) to hydrophobic (isoleucine [Ile]). Image published in: Niedzialkowska E et al. (2012) © 2012 Niedzialkowska et al. This image is reproduced with permission of the journal and the copyright holder. This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike license Larger Image Printer Friendly View

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