3EXL

Crystal structure of a p53 core tetramer bound to DNA.

(2009) Oncogene 28: 325-333

• PubMed: 18978813 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.1038/onc.2008.400
• Primary Citation of Related Structures:  
  3EXJ, 3EXL


• PubMed Abstract: 
  

  The tumor suppressor p53 regulates downstream genes in response to many cellular stresses and is frequently mutated in human cancers. Here, we report the use of a crosslinking strategy to trap a tetrameric p53 DNA-binding domain (p53DBD) bound to DNA and the X-ray crystal structure of the protein/DNA complex. The structure reveals that two p53DBD dimers bind to B form DNA with no relative twist and that a p53 tetramer can bind to DNA without introducing significant DNA bending. The numerous dimer-dimer interactions involve several strictly conserved residues, thus suggesting a molecular basis for p53DBD-DNA binding cooperativity. Surface residue conservation of the p53DBD tetramer bound to DNA highlights possible regions of other p53 domain or p53 cofactor interactions.

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Organizational Affiliation: 

The Wistar Institute, Philadelphia, PA 19104, USA.