Supplementary Figure 2. Two-Directional 3D-Structural View of the P53 Tetramerization

Kawaguchi et al.

Supplementary Figure 1. Three-directional 3D-structural view of the p53 tetramerization domain on monomer-monomer interaction. p53 homo-tetramer consists of p53 (a), p53 (b), p53 (c) and p53 (d) molecules. Residues shown in A, B and C were involved in p53 (a) (yellow) and p53 (c) (purple) interaction. These residues contact each other and form hydrophobic core between p53 (a) and p53 (c). Apparently, these are residues in which one or more the p53 mutants were monomer mutants. Role of R333, R342 and R347 on dimer-dimer interaction were not elucidated by the structure-based analysis. Because the monomer mutations in these residues were only proline substitution (R333P, R342P and A347P), the mutants may destroy the backbone structure of b-strand and a-helix rather.

Supplementary Figure 2. Two-directional 3D-structural view of the p53 tetramerization domain on dimer-dimer interaction. p53 homo-tetramer consists of p53 (a/c) dimmer and p53 (b/d) dimer molecules. Residues shown in A and B were involved in p53 (a) (yellow) and p53 (b) (light blue) interaction. These residues contact each other and form hydrophobic core between p53 (a) and p53 (b). Only M340 was involved in p53 (a) and p53 (d) or p53 (b) and p53 (c) interaction (B, upper panel). Apparently, these are residues in which one or more the p53 mutants were dimer mutants. Role of D352 and A353 on dimer-dimer interaction were not clarified by the structure-based analysis (A, upper and lower panels).

Supplementary Figure 3. Phylogenetic analysis of the p53 protein family. Analysis of the amino-acid alignment of full-length p53 from Bos taurus (cow), Gallus gallus (chicken), Oncorhynchus mykiss (rainbow trout), Xenopus laevis (African clawed frog) and Loligo forbesi (northern European squid) was performed using AlignX, Vector NTI Suite (InforMax) and the result of the COOH-terminal part (residues 322-358) is shown. Red: residues perfectly matched among the eight p53 members. Blue: residues matched among more than 5 members. Yellow: well-conserved residues among more than 5 members.

2