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Structure of simian virus 40 at 3.8-Å resolution

Nature volume 354, pages 278–284 (1991)Cite this article

Abstract

The crystallographically determined structure of simian virus 40 shows that the 72 pentamers of viral protein VP1, which form the outer shell, have identical conformations except for the C-terminal arms of their subunits. Five arms emerge from each pentamer and insert into neighbouring pentamers. This tying together of standard building blocks allows for the required variability in packing geometry without sacrificing specificity.

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Author notes

  1. R. C. Liddington

    Present address: Dana Farber Cancer Institute, 44 Binney Street, Boston, Massachusetts, 02115, USA

  2. J. Moulai

    Present address: Brandeis University, 415 South Street, Waltham, Massachusetts, 02154, USA

  3. R. Sahli

    Present address: Institute of Microbiology CHUV, Lausanne, Switzerland

Authors and Affiliations

  1. Howard Hughes Medical Institute, Harvard University, Cambridge, Massachusetts, 02138, USA

    R. C. Liddington, Y. Yan & S. C. Harrison

  2. Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts, 02138, USA

    R. C. Liddington, Y. Yan, J. Moulai & S. C. Harrison

  3. Department of Pathology, Harvard Medical School, Boston, Massachusetts, 02115, USA

    R. Sahli & T. L. Benjamin

Authors
  1. R. C. Liddington
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  2. Y. Yan
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  3. J. Moulai
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  4. R. Sahli
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  5. T. L. Benjamin
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  6. S. C. Harrison
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Liddington, R., Yan, Y., Moulai, J. et al. Structure of simian virus 40 at 3.8-Å resolution. Nature 354, 278–284 (1991). https://doi.org/10.1038/354278a0

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