Journal
ONCOGENE
Volume 28, Issue 3, Pages 325-333Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/onc.2008.400
Keywords
p53; tumor suppressor; protein/DNA complex; crystal structure
Funding
- NIGMS NIH HHS [R01 GM052880, R01 GM052880-11, T32 GM008275] Funding Source: Medline
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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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