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Structure of measles virus hemagglutinin bound to its epithelial receptor nectin-4.
MedLine Citation:
PMID:  23202587     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
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.
Authors:
Xiaoai Zhang; Guangwen Lu; Jianxun Qi; Yan Li; Yan He; Xiang Xu; Jia Shi; Catherine W-H Zhang; Jinghua Yan; George F Gao
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-12-02
Journal Detail:
Title:  Nature structural & molecular biology     Volume:  -     ISSN:  1545-9985     ISO Abbreviation:  Nat. Struct. Mol. Biol.     Publication Date:  2012 Dec 
Date Detail:
Created Date:  2012-12-3     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101186374     Medline TA:  Nat Struct Mol Biol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
1] CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China. [2].
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