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