• Biology, Medicine
• Published in The EMBO journal 2006
• DOI:10.1038/sj.emboj.7601382

The structure of p53 tumour suppressor protein reveals the basis for its functional plasticity.

@article{Okorokov2006TheSO,
  title={The structure of p53 tumour suppressor protein reveals the basis for its functional plasticity.},
  author={Andrei L. Okorokov and Michael B. Sherman and C{\'e}lia Plisson and Vera Grinkevich and Kristmundur Sigmundsson and Galina A. Selivanova and Jo Milner and Elena V Orlova},
  journal={The EMBO journal},
  year={2006},
  volume={25 21},
  pages={
          5191-200
        }
}

• Andrei L. Okorokov, Michael B. Sherman, +5 authors Elena V Orlova

p53 major tumour suppressor protein has presented a challenge for structural biology for two decades. The intact and complete p53 molecule has eluded previous attempts to obtain its structure, largely due to the intrinsic flexibility of the protein. Using ATP-stabilised p53, we have employed cryoelectron microscopy and single particle analysis to solve the first three-dimensional structure of the full-length p53 tetramer (resolution 13.7 A). The p53 molecule is a D2 tetramer, resembling a… CONTINUE READING

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