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	Structures of the n- and c-terminal domains of mhv-a59 nucleocapsid protein corroborate a conserved rna-protein binding mechanism in coronavirus
	Ma, Yanlin1,2; Tong, Xiaohang1,2; Xu, Xiaoling3; Li, Xuemei1; Lou, Zhiyong3; Rao, Zihe1,3
刊名	Protein & cell
	2010-07-01
卷号	1期号:7页码:688-697
关键词	Crystal structure Nucleocapsid protein Murine hepatitis virus
ISSN号	1674-800X
DOI	10.1007/s13238-010-0079-x
通讯作者	Rao, zihe(raozh@xtal.tsinghua.edu.cn)
英文摘要	Coronaviruses are the causative agent of respiratory and enteric diseases in animals and humans. one example is sars, which caused a worldwide health threat in 2003. in coronaviruses, the structural protein n (nucleocapsid protein) associates with the viral rna to form the filamentous nucleocapsid and plays a crucial role in genome replication and transcription. the structure of n-terminal domain of mhv n protein also implicated its specific affinity with transcriptional regulatory sequence (trs) rna. here we report the crystal structures of the two proteolytically resistant n- (ntd) and c-terminal (ctd) domains of the n protein from murine hepatitis virus (mhv). the structure of ntd in two different crystal forms was solved to 1.5 angstrom. the higher resolution provides more detailed structural information than previous reports, showing that the ntd structure from mhv shares a similar overall and topology structure with that of sars-cov and ibv, but varies in its potential surface, which indicates a possible difference in rna-binding module. the structure of ctd was solved to 2.0-angstrom resolution and revealed a tightly intertwined dimer. this is consistent with analytical ultracentrifugation experiments, suggesting a dimeric assembly of the n protein. the similarity between the structures of these two domains from sars-cov, ibv and mhv corroborates a conserved mechanism of nucleocapsid formation for coronaviruses.
WOS研究方向	Cell Biology
WOS类目	Cell Biology
语种	英语
出版者	HIGHER EDUCATION PRESS
WOS记录号	WOS:000208511100011
内容类型	期刊论文
URI标识	http://www.corc.org.cn/handle/1471x/2412194
专题	中国科学院大学
通讯作者	Rao, Zihe
作者单位	1.Chinese Acad Sci, Inst Biophys, Life Natl Lab Biomacromol, Beijing 100101, Peoples R China 2.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China 3.Tsinghua Univ, Struct Biol Lab, Beijing 100084, Peoples R China
推荐引用方式 GB/T 7714	Ma, Yanlin,Tong, Xiaohang,Xu, Xiaoling,et al. Structures of the n- and c-terminal domains of mhv-a59 nucleocapsid protein corroborate a conserved rna-protein binding mechanism in coronavirus[J]. Protein & cell,2010,1(7):688-697.
APA	Ma, Yanlin,Tong, Xiaohang,Xu, Xiaoling,Li, Xuemei,Lou, Zhiyong,&Rao, Zihe.(2010).Structures of the n- and c-terminal domains of mhv-a59 nucleocapsid protein corroborate a conserved rna-protein binding mechanism in coronavirus.Protein & cell,1(7),688-697.
MLA	Ma, Yanlin,et al."Structures of the n- and c-terminal domains of mhv-a59 nucleocapsid protein corroborate a conserved rna-protein binding mechanism in coronavirus".Protein & cell 1.7(2010):688-697.

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