Comparison of the protein-protein interfaces in the p53-DNA crystal structures: towards elucidation of the biological interface.

ABSTRACT: p53, the tumor suppressor protein, functions as a dimer of dimers. However, how the tetramer binds to the DNA is still an open question. In the crystal structure, three copies of the p53 monomers (containing chains A, B, and C) were crystallized with the DNA-consensus element. Although the structure provides crucial data on the p53-DNA contacts, the active oligomeric state is unclear because the two dimeric (A-B and B-C) interfaces present in the crystal cannot both exist in the tetramer. Here, we address the question of which of these two dimeric interfaces may be more biologically relevant. We analyze the sequence and structural properties of the p53-p53 dimeric interfaces and carry out extensive molecular dynamics simulations of the crystal structures of the human and mouse p53 dimers.

SUBMITTER: Ma B 

PROVIDER: S-EPMC554805 | biostudies-literature | 2005 Mar

REPOSITORIES: biostudies-literature