Figure 1
(a–c) The 3D structure model of p53 is shown here in its tetramer form bound to a full DNA consensus site extracted from the MD simulation. The four monomers are coloured in black, red, green and blue. The 18 bp DNA structure is coloured in purple. (d) Per-residue root-mean-square fluctuations (RMSFs) for each p53 monomer (colours as in a–c). Arrows highlight the residues belonging to the DBD, the tetramerization domain (TET) and the tetramerization helix (TE). As previously described for full-length p53,13 the DBD region is significantly more rigid, with relatively low RMSF values. (e) Secondary structure as a function of simulation time. The four monomers (M1–M4) show a very stable structure over time in the DBD and TE, whereas specific regions are able to switch between α-helix (blue), turn (yellow) and bend (green).
