The oligomerization domain of p53: crystal structure of the trigonal form

FEBS Lett. 1996 Dec 9;399(1-2):166-70. doi: 10.1016/s0014-5793(96)01231-8.


The structure of the oligomerization domain of the p53 tumor suppressor protein was determined in the trigonal crystal form, using a refined NMR structure as a model. A synthetic peptide comprising residues 319-360 of human p53 crystallized in the space group P3(1)21. There is one biologically relevant tetrameric domain in the crystallographic asymmetric unit. The structure was refined jointly with NMR data, only the third such case (the previous examples being IL-1beta (Shaanan, B., Gronenborn, A.M., Cohen, G.H., Gilliland, G.L., Veerapandian, B., Davies, D.R. and Clore, G.M. (1992) Science 257, 961-964 [1]) and BPTI (Schiffer, C., Huber, R., Wuthrich, K. and Van Gunsteren, W.F. (1994) J. Mol. Biol. 241, 588-599 [21)), to 2.5 A resolution with an R factor of 0.207. The distribution of tumor-derived mutations in the oligomerization region together with structural and biological data suggest a strategy for the design of antitumor therapeutics.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Biopolymers
  • Crystallography, X-Ray
  • Humans
  • Magnetic Resonance Spectroscopy
  • Protein Conformation
  • Tumor Suppressor Protein p53 / chemistry*


  • Biopolymers
  • Tumor Suppressor Protein p53