Nature 354, 278 - 284 (28 November 1991); doi:10.1038/354278a0

Structure of simian virus 40 at 3.8-Å resolution

R. C. Liddington^*†‡, Y. Yan^*†, J. Moulai^†‡, R. Sahli^§‡, T. L. Benjamin^§ & S. C. Harrison^*†

^*Howard Hughes Medical Institute and ^† Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts 02138, USA
^§Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115, USA
^‡Present addresses: Dana Farber Cancer Institute, 44 Binney Street, Boston, Massachusetts 02115, USA (R.C.L.); Brandeis University, 415 South Street, Waltham, Massachusetts 02154, USA (J.M.); Institute of Microbiology CHUV, Lausanne, Switzerland (R.S.).

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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