| 论文题目: | Structure of measles virus hemagglutinin bound to its epithelial receptor nectin-4 |
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| 作者: | Zhang Xiaoai, Lu Guangwen, Qi Jianxun, Li Yan, He Yan, Xu Xiang, Shi Jia, Zhang Catherine, W-H, Yan Jinghua, George F. Gao |
| 联系作者: | George F. Gao |
| 刊物名称: | Nature Structural & Molecular Biology |
| 期: | 1 |
| 卷: | 20 |
| 页: | 67-U86 |
| 年份: | 2013 |
| 影响因子: | 12.114 |
| 论文下载: | 下载地址 |
| 摘要: | Measles virus is a major public health concern worldwide. Three measles virus cell receptors have been identified so far, and the structures of the first two in complex with measles virus hemagglutinin (MV-H) have been reported. Nectin-4 is the most recently identified receptor in epithelial cells, and its binding mode to MV-H remains elusive. In this study, we solved the structure of the membrane-distal domain of human nectin-4 in complex with MV-H. The structure shows that nectin-4 binds the MV-H beta 4-beta 5 groove exclusively via its N-terminal IgV domain; the contact interface is dominated by hydrophobic interactions. The binding site in MV-H for nectin-4 also overlaps extensively with those of the other two receptors. Finally, a hydrophobic pocket centered in the beta 4-beta 5 groove is involved in binding to all three identified measles virus receptors, representing a potential target for antiviral drugs. |
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