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Solution structure of the tetrameric minimum transforming domain of p53

Nature Structural Biology volume 1, pages 877–890 (1994)Cite this article

An Erratum to this article was published on 01 January 1995

Abstract

We report the solution structure of the minimum transforming domain (residues 303–366) of human p53 (p53tet) determined by multidimensional NMR spectroscopy. This domain contains a number of important functions associated with p53 activity including transformation, oligomerization, nuclear localization and a phosphorylation site for p34/cdc2 kinase. p53tet forms a symmetric dimer of dimers that is significantly different from a recent structure reported for a shorter construct of this domain. Phosphorylation of Ser 315 has only minor structural consequences, as this region of the protein is unstructured. Modelling based on the p53tet structure suggests possible modes of interaction between adjacent domains in full-length p53 as well as modes of interaction with DNA.

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  1. Timothy S. Harvey

    Present address: AMGEN, Inc. Mail Stop 14-2-A-210, 1840 Deltavilland Drive, Thousand Oaks, California, 91320, USA

Authors and Affiliations

  1. Division of Molecular and Structural Biology, Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, 500 Sherbourne Street, Toronto, Ontario, M5X 1K9, Canada

    Weontae Lee, Timothy S. Harvey, Ya Yin, Patrick Yau & Cheryl H. Arrowsmith

  2. Manitoba Institute of Cell Biology, 100 Olivia Street, Winnipeg, Manitoba, R3E 0V9, Canada

    David Litchfield

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Lee, W., Harvey, T., Yin, Y. et al. Solution structure of the tetrameric minimum transforming domain of p53. Nat Struct Mol Biol 1, 877–890 (1994). https://doi.org/10.1038/nsb1294-877

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