Author: Xu, Xiaoling; Lou, Zhiyong; Ma, Yanlin; Chen, Xuehui; Yang, Zhangsheng; Tong, Xiaohang; Zhao, Qi; Xu, Yuanyuan; Deng, Hongyu; Bartlam, Mark; Rao, Zihe
Title: Crystal Structure of the C-Terminal Cytoplasmic Domain of Non-Structural Protein 4 from Mouse Hepatitis Virus A59 Document date: 2009_7_10
ID: 1beonuh7_29
Snippet: Multiple sequence alignment of MHV-A59 nsp4 with representatives from all three groups of the genus Coronavirus reveals that the membrane topology of nsp4 from all group members is similar. In particular, the C-terminal hydrophilic region from T408 to Q496 is highly conserved among all the coronaviruses (Fig. 4B) , indicating that nsp4C may play a similar and conserved role in coronavirus replication. In summary, the crystal structure of MHV-A59 .....
Document: Multiple sequence alignment of MHV-A59 nsp4 with representatives from all three groups of the genus Coronavirus reveals that the membrane topology of nsp4 from all group members is similar. In particular, the C-terminal hydrophilic region from T408 to Q496 is highly conserved among all the coronaviruses (Fig. 4B) , indicating that nsp4C may play a similar and conserved role in coronavirus replication. In summary, the crystal structure of MHV-A59 nsp4C reported here provides a preliminary structural description of coronavirus non-structural protein nsp4, further functional and structural studies of nsp4, together with its interaction with other virus and host cell proteins, will certainly boost our understanding the role of nsp4 in coronavirus replication.
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