We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Structure of measles virus hemagglutinin bound to its epithelial receptor nectin-4.
- Authors
Zhang, Xiaoai; Lu, Guangwen; Qi, Jianxun; Li, Yan; He, Yan; Xu, Xiang; Shi, Jia; Zhang, Catherine W-H; Yan, Jinghua; Gao, George F
- Abstract
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 ?4-?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 ?4-?5 groove is involved in binding to all three identified measles virus receptors, representing a potential target for antiviral drugs.
- Subjects
MEASLES virus; HEMAGGLUTININ; EPITHELIAL cells; NECTINS; CELL receptors; ANTIVIRAL agents
- Publication
Nature Structural & Molecular Biology, 2013, Vol 20, Issue 1, p67
- ISSN
1545-9993
- Publication type
Article
- DOI
10.1038/nsmb.2432