Structures of the n- and c-terminal domains of mhv-a59 nucleocapsid protein corroborate a conserved rna-protein binding mechanism in coronavirus
文献类型：期刊论文
| 作者 | Ma, Yanlin1,2; Tong, Xiaohang1,2; Xu, Xiaoling3; Li, Xuemei1; Lou, Zhiyong3; Rao, Zihe1,3 |
| 刊名 | Protein & cell
 |
| 出版日期 | 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 |
| WOS记录号 | WOS:000208511100011 |
| 出版者 | HIGHER EDUCATION PRESS |
| URI标识 | http://www.irgrid.ac.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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来源：中国科学院大学
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