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Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms

P D Jeffrey1, S Gorina, N P Pavletich

  • 1Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021.

Science (New York, N.Y.)
|March 10, 1995
PubMed

Insights

The p53 protein

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Cancer Research

Background:

  • The p53 protein is a crucial transcription factor involved in preventing cancer.
  • Its tumor-suppressing activity is dependent on its ability to form a tetramer.
  • Oligomerization-deficient p53 mutants fail to inhibit carcinoma cell growth.

Purpose of the Study:

  • To determine the crystal structure of the p53 tetramerization domain.
  • To elucidate the molecular basis of p53 tetramer formation.
  • To understand how the structure relates to p53's tumor-suppressing function.

Main Methods:

  • X-ray crystallography was used to determine the structure of the p53 tetramerization domain (residues 325-356).
  • The structure was resolved to 1.7 angstrom resolution.
  • Refinement was performed to a crystallographic R factor of 19.2%.

Main Results:

  • The crystal structure reveals the atomic details of the p53 tetramerization domain.
  • A monomer consists of a beta strand and an alpha helix.
  • Monomers dimerize via antiparallel beta sheet and helix-helix interfaces; two dimers then associate via a parallel helix-helix interface to form the tetramer.

Conclusions:

  • The determined structure provides a molecular understanding of p53 tetramer formation.
  • This structural insight is essential for understanding the mechanism of p53's tumor suppressor activity.
  • The findings highlight the importance of oligomerization for p53's function in preventing neoplastic transformation.

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