西亚试剂：：Structure of measles virus hemagglutinin

Xiaoai Zhang,1, 6 Guangwen Lu,1, 6 Jianxun Qi,1 Yan Li,1 Yan He,2 Xiang Xu,3 Jia Shi,2 Catherine W-H Zhang,2 Jinghua Yan1 & George F Gao1, 4, 5

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 β4-β5 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 β4-β5 groove is involved in binding to all three identified measles virus receptors, representing a potential target for antiviral drugs.

丙烯醛肉桂醛桂皮醛4-硝基肉桂醛