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Structure of the reovirus core at 3.6?Å resolution

Author

Listed:
  • Karin M. Reinisch

    (Harvard University and)

  • Max L. Nibert

    (Department of Biochemistry and Institute for Molecular Virology
    University of Wisconsin-Madison)

  • Stephen C. Harrison

    (Harvard University and
    Howard Hughes Medical Institute, Fairchild Building)

Abstract

The reovirus core is an assembly with a relative molecular mass of 52 million that synthesizes, modifies and exports viral messenger RNA. Analysis of its structure by X-ray crystallography shows that there are alternative, specific and completely non-equivalent contacts made by several surfaces of two of its proteins; that the RNA capping and export apparatus is a hollow cylinder, which probably sequesters its substrate to ensure completion of the capping reactions; that the genomic double-stranded RNA is coiled into concentric layers within the particle; and that there is a protein shell that appears to be common to all groups of double-stranded RNA viruses.

Suggested Citation

  • Karin M. Reinisch & Max L. Nibert & Stephen C. Harrison, 2000. "Structure of the reovirus core at 3.6?Å resolution," Nature, Nature, vol. 404(6781), pages 960-967, April.
    • Handle: RePEc:nat:nature:v:404:y:2000:i:6781:d:10.1038_35010041
    DOI: 10.1038/35010041
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    Cited by:

    1. Zhiqiang Li & Han Xia & Guibo Rao & Yan Fu & Tingting Chong & Kexing Tian & Zhiming Yuan & Sheng Cao, 2024. "Cryo-EM structures of Banna virus in multiple states reveal stepwise detachment of viral spikes," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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