It was expected that there are a coil (289～325) and two α helix (α₁ 368～373,α₂ 381～388) structures in p53 protein C-terminal region based on its mRNA secondary structure template and Chou-Fasman's protein secondary structure principle of prediction. The result was conformed by the other four methods of protein secondary structure prediction that are based on the multiple sequence alignment (accuracy=73.20%). Combine with the 31 amino acids crystal structure of the oligomerization, the three dimensional conformation of p53 C-terminal 108 residues was built using the SGI INDIGO² computer. This structure further expounds the relationship among those biological function domains of p53 C-terminus at three-dimensional level.