QQ客服 官方微博 反馈留言

	Electron cryomicroscopy and bioinformatics suggest protein fold models for rice dwarf virus
	Zhou, ZH ; Baker, ML ; Jiang, W ; Dougherty, M ; Jakana, J ; Dong, G ; Lu, GY ; Chiu, W
	2001
关键词	STRUCTURE PREDICTION CORE CRYSTALLOGRAPHY VISUALIZATION PHYTOREOVIRUS RESOLUTION ANGSTROM SERVER
DOI	10.1038/nsb1001-868
英文摘要	The three-dimensional structure of rice dwarf virus was determined to 6.8 Angstrom resolution by single particle electron cryomicroscopy. By integrating the structural analysis with bioinformatics, the folds of the proteins in the double-shelled capsid were derived. In the outer shell protein, the uniquely orientated upper and lower domains are composed of similar secondary structure elements but have different relative orientations from that of bluetongue virus in the same Reoviridae family. Differences in both sequence and structure between these proteins may be important in defining virus-host interactions. The inner shell protein adopts a conformation similar to other members of Reoviridae, suggesting a common ancestor that has evolved to infect hosts ranging from plants to animals. Symmetry mismatch between the two shells results in nonequivalent, yet specific, interactions that contribute to the stability of this large macromolecular machine.; Biochemistry & Molecular Biology; Biophysics; Cell Biology; SCI(E); 103; ARTICLE; 10; 868-873; 8
语种	英语
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/401830]
专题	生命科学学院
推荐引用方式 GB/T 7714	Zhou, ZH,Baker, ML,Jiang, W,et al. Electron cryomicroscopy and bioinformatics suggest protein fold models for rice dwarf virus[J],2001.
APA	Zhou, ZH.,Baker, ML.,Jiang, W.,Dougherty, M.,Jakana, J.,...&Chiu, W.(2001).Electron cryomicroscopy and bioinformatics suggest protein fold models for rice dwarf virus..
MLA	Zhou, ZH,et al."Electron cryomicroscopy and bioinformatics suggest protein fold models for rice dwarf virus".(2001).

个性服务

查看访问统计

相关权益政策

暂无数据

收藏/分享

除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。