Structure of the human p53 core domain in the absence of DNA.

@article{Wang2007StructureOT,
  title={Structure of the human p53 core domain in the absence of DNA.},
  author={Ying Wang and Anja Rosengarth and Hartmut Luecke},
  journal={Acta crystallographica. Section D, Biological crystallography},
  year={2007},
  volume={63 Pt 3},
  pages={276-81}
}
The tumor suppressor protein p53 plays a key role in cell-cycle regulation by triggering DNA repair, cell-cycle arrest and apoptosis when the appropriate signal is received. p53 has the classic architecture of a transcription factor, with an amino-terminal transactivation domain, a core DNA-binding domain and carboxy-terminal tetramerization and regulatory domains. The crystal structure of the p53 core domain, which includes the amino acids from residue 96 to residue 289, has been determined in… CONTINUE READING

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