RGD Reference Report - Structural basis of DNA recognition by p53 tetramers. - Rat Genome Database

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Structural basis of DNA recognition by p53 tetramers.

Authors: Kitayner, M  Rozenberg, H  Kessler, N  Rabinovich, D  Shaulov, L  Haran, TE  Shakked, Z 
Citation: Kitayner M, etal., Mol Cell. 2006 Jun 23;22(6):741-53.
RGD ID: 5129869
Pubmed: PMID:16793544   (View Abstract at PubMed)
DOI: DOI:10.1016/j.molcel.2006.05.015   (Journal Full-text)

The tumor-suppressor protein p53 is among the most effective of the cell's natural defenses against cancer. In response to cellular stress, p53 binds as a tetramer to diverse DNA targets containing two decameric half-sites, thereby activating the expression of genes involved in cell-cycle arrest or apoptosis. Here we present high-resolution crystal structures of sequence-specific complexes between the core domain of human p53 and different DNA half-sites. In all structures, four p53 molecules self-assemble on two DNA half-sites to form a tetramer that is a dimer of dimers, stabilized by protein-protein and base-stacking interactions. The protein-DNA interface varies as a function of the specific base sequence in correlation with the measured binding affinities of the complexes. The new data establish a structural framework for understanding the mechanisms of specificity, affinity, and cooperativity of DNA binding by p53 and suggest a model for its regulation by regions outside the sequence-specific DNA binding domain.


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