Structure of the reovirus core at 3.6 Å resolution

被引：367

作者：

Reinisch, KM

Nibert, M

Harrison, SC ^{[1
]}

机构：

[1] Harvard Univ, Fairchild Bldg,7 Divin Ave, Cambridge, MA 02138 USA

[2] Howard Hughes Med Inst, Cambridge, MA 02138 USA

[3] Univ Wisconsin, Dept Biochem, Madison, WI 53706 USA

[4] Univ Wisconsin, Inst Mol Virol, Madison, WI 53706 USA

来源：

NATURE | 2000年 / 404卷 / 6781期

关键词：

D O I：

10.1038/35010041

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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 nonequivalent 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.

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页码：960 / 967

页数：8

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