Crystal structure of the β-catenin/ICAT complex.
- Publication date
- Publisher
Abstract
<p><b>A</b> Crystal structure of ICAT bound to the core domain of β-catenin (PDB code 1LUJ,[<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0172603#pone.0172603.ref022" target="_blank">22</a>]). ICAT is shown as yellow ribbons and β-catenin as purple cylinders. The secondary structures were calculated using the program STRIDE [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0172603#pone.0172603.ref037" target="_blank">37</a>]. Residues mutated in this study are shown as hard spheres. ICAT residues are colored according to their characteristics: white for hydrophobic, green for polar, red for acidic and blue for basic residues. β-catenin F660 is in pink and the basic residues facing the C-terminal domain of ICAT are in cyan. <b>B</b>. Sequence alignment of the consensus peptide from several β-catenin binding proteins. The conserved acidic residues are in red and the aromatic residue in green. The first X residues, when they are hydrophilic, are boxed. <b>C</b>. β-catenin/ICAT complex showing the interaction between ICAT consensus peptide of the C-terminal domain (ribbon and sticks) and its facing β-catenin residues (surface). All residues are colored according to their characteristics. Figures were drawn using VMD software [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0172603#pone.0172603.ref038" target="_blank">38</a>].</p