Comparison of the protein-protein interfaces in the p53-DNA crystal structures: towards elucidation of the biological interface.

@article{Ma2005ComparisonOT,
  title={Comparison of the protein-protein interfaces in the p53-DNA crystal structures: towards elucidation of the biological interface.},
  author={Buyong Ma and Yongping Pan and Kannan Gunasekaran and R Babu Venkataraghavan and Arnold J. Levine and Ruth Nussinov},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2005},
  volume={102 11},
  pages={
          3988-93
        }
}
p53, the tumor suppressor protein, functions as a dimer of dimers. However, how the tetramer binds to the DNA is still an open question. In the crystal structure, three copies of the p53 monomers (containing chains A, B, and C) were crystallized with the DNA-consensus element. Although the structure provides crucial data on the p53-DNA contacts, the active oligomeric state is unclear because the two dimeric (A-B and B-C) interfaces present in the crystal cannot both exist in the tetramer. Here… CONTINUE READING

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