Fig. 1
From: p53: from understanding its structure to advances in therapeutic targeting
The main domain structure of the full-length p53 protein and the structures of p53 and MDM2/4. a The p53 protein in humans is composed of five distinct domains: the transactivation domain (TAD, AA 1–61), the proline-rich domain (PRD, AA 62–94), the central DNA-binding domain (DBD, AA 95–292), the tetramerization domain (TD, AA 325–356), and the C-terminal regulatory domain (CTD, AA 357–393). A linker region (LR) links the DBD to the TD. AA: amino acid. b p53 monomer structure and 6 hotpots (PDB: 8F2I). c Structure of the human MDMX protein bound to the p53 tumor suppressor transactivation domain (PDB: 3DAB). d MDM2 bound to the transactivation domain of p53 (PDB: 1YCR). e MDMX is shown as a surface (PDB: 3DAB). f MDM2 is shown as a surface (PDB: 1YCR). This figure was created by BioRender.com
