期刊
SCIENCE
卷 329, 期 5995, 页码 1038-1043出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1187433
关键词
-
资金
- National Institutes of Health [GM071940, AI069015, CA101904, 1S10RR23057]
- National Natural Scientific Foundation of China [10874144]
- Congressionally Directed Medical Research Programs [W81XWH-06-1-055]
Construction of a complex virus may involve a hierarchy of assembly elements. Here, we report the structure of the whole human adenovirus virion at 3.6 angstroms resolution by cryo-electron microscopy (cryo-EM), revealing in situ atomic models of three minor capsid proteins (IIIa, VIII, and IX), extensions of the (penton base and hexon) major capsid proteins, and interactions within three protein-protein networks. One network is mediated by protein IIIa at the vertices, within group-of-six (GOS) tiles-a penton base and its five surrounding hexons. Another is mediated by ropes (protein IX) that lash hexons together to form group-of-nine (GON) tiles and bind GONs to GONs. The third, mediated by IIIa and VIII, binds each GOS to five surrounding GONs. Optimization of adenovirus for cancer and gene therapy could target these networks.
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