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  • Title: Sequence-specific interaction of a conformational domain of p53 with DNA.
    Author: Srinivasan R, Roth JA, Maxwell SA.
    Journal: Cancer Res; 1993 Nov 15; 53(22):5361-4. PubMed ID: 8221671.
    Abstract:
    Mutations within a conserved "conformational" domain of the p53 protein have frequently been observed in a wide variety of human cancers. A hybrid protein containing the wild-type conformational domain of p53 fused to protein A bound to calf thymus DNA and a specific p53 DNA-binding motif. Hybrid proteins containing mutations in p53 bound to DNA less efficiently than wild-type hybrid protein. In addition, competition experiments showed that mutated p53 DNA-binding motif failed to interact with p53 hybrid proteins. The DNA-binding activity of wild-type p53 hybrid protein was inhibited by the metal chelator 1,10-phenanthroline. These results demonstrate that DNA-binding activity resides in the conformational domain of p53, providing a structural model for disruption of DNA binding by mutation. Furthermore, metal ions may regulate binding of p53 to DNA by modulating its conformation.
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