Skip to main content
. 2016 May 26;6:26707. doi: 10.1038/srep26707

Figure 2. Structural homology and stability of p63-DBD and p53-DBD.

Figure 2

(a) Multiple sequence alignment of p53-family proteins. Secondary structural elements in p63-DBD are indicated. p53-DBD and p63-DBD share a 55% sequence identity. (b) The solution structures of p63-DBD (left) and p53-DBD (right) show the same structural topology and secondary structure content. (c) CD-detected thermal unfolding traces of both proteins reveal a large difference in thermal stability between p63-DBD (red, 65 °C) and p53-DBD (blue, 43 °C). (d) Packing of amino acid side chains in the hydrophobic core of p63 (red) and p53 (blue). Spheres within p53-DBD indicate unfavorable cavities. (e) The protein core of p63-DBD is tightly packed by hydrophobic side chains. Labeled amino acids correspond to positions in p53-DBD that have been mutated by rational design. (f) p53-DBD is less tightly packed with hydrophobic amino acids. The indicated amino acids have been mutated to the corresponding residues in p63-DBD in order to enhance protein stability.