期刊
STRUCTURE
卷 13, 期 10, 页码 1545-1557出版社
CELL PRESS
DOI: 10.1016/j.str.2005.07.012
关键词
-
资金
- NCI NIH HHS [R37 CA013202, R01 CA013202, R01 CA13202] Funding Source: Medline
- NIAID NIH HHS [R01 AI46440, R01 AI047904, R01 AI046440, R01 AI47904, P01 AI045976] Funding Source: Medline
- NIGMS NIH HHS [R01 GM33050, R01 GM62580, R37 GM033050, R01 GM033050, P01 GM062580] Funding Source: Medline
Reovirus is a useful model for addressing the molecular basis of membrane penetration by one of the larger nonenveloped animal viruses. We now report the structure of the reovirus virion at 7.0 angstrom resolution as obtained by electron cryomicroscopy and three-dimensional image reconstruction. Several features of the myristoylated outer capsid protein mu 1, not seen in a previous X-ray crystal structure of the mu 1-sigma 3 heterohexamer, are evident in the virion. These features appear to be important for stabilizing the outer capsid, regulating the conformational changes in mu 1 that accompany perforation of target membranes, and contributing directly to membrane penetration during cell entry.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据