The N-terminal region is dynamically disordered in the full-length p53 tetramer fluctuating between states in which it is free and fully exposed to solvent and states in which it makes transient contacts with the DNA-binding domain.
Structure determination of the transactivation domains of p63 and p73 in complex with the p300 Taz2 domain further revealed that in contrast to p53 and p73 p63 has a single transactivation domain.
This finding expands the universe of p53 binding sites and demonstrates that even isolated p53 half-sites can form tetrameric complexes. Moreover it explains the manner in which p53 binds to clusters of more than one canonical binding site common in many natural REs.
crystal structure of a ternary complex comprising full-length human papilloma virus type 16 (HPV-16) E6 the LxxLL motif of E6AP and the core domain of p53
Data from studies using peptide fragments suggest that complexes formed by the two transcriptional subdomains of TP53 with EP300 (histone acetyltransferase p300) exhibit different conformations and play roles in TP53 transcriptional activity.
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