Structure of the reovirus core at 3.6?Å resolution

Karin M. Reinisch, Max L. Nibert and Stephen C. Harrison ()
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Karin M. Reinisch: Harvard University and
Max L. Nibert: Department of Biochemistry and Institute for Molecular Virology
Stephen C. Harrison: Harvard University and

Nature, 2000, vol. 404, issue 6781, 960-967

Abstract: 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.

Date: 2000
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DOI: 10.1038/35010041

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