title: Structure of the reovirus core at 3.6 A resolution.
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.
authors.affiliation: Harvard University, Cambridge, Massachusetts 02138, USA.
authors.forename: K M
authors.initials: KM
authors.lastname: Reinisch
authors.forename: M L
authors.initials: ML
authors.lastname: Nibert
authors.forename: S C
authors.initials: SC
authors.lastname: Harrison
mesh_terms: D002213:Capsid / Q000737:chemistry*; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D011487:Protein Conformation; D012315:RNA Caps; D012330:RNA, Double-Stranded / Q000737:chemistry; D012367:RNA, Viral / Q000737:chemistry; D012087:Reoviridae / Q000737:chemistry*
chemical_list: D012315:RNA Caps; D012330:RNA, Double-Stranded; D012367:RNA, Viral