3inb
Structure of the measles virus hemagglutinin bound to the CD46 receptor
Structural highlights
FunctionHEMA_MEASE Attaches the virus to cell receptors and thereby initiating infection. Binding of H protein to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion. May use human CD46 and/or SLAMF1 as receptors for viral entry into the cell. The high degree of interaction between H and MCP/CD46 results in down-regulation of the latter from the surface of infected cells, rendering them more sensitive to c3b-mediated complement lysis.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe highly contagious measles virus infects millions of individuals worldwide, causing serious disease in children of developing countries. Infection is initiated by attachment of the measles virus hemagglutinin (MV-H), a glycoprotein anchored to the virus envelope, to the host cell receptors CD46 or signaling lymphocyte activation molecule (SLAM). Here we report the crystal structure of MV-H in complex with a CD46 protein spanning the two N-terminal domains. A unique groove at the side of the MV-H beta-propeller domain, which is absent in homologous paramyxovirus attachment proteins, engages residues in both CD46 domains. Key contacts involve a protruding loop in the N-terminal CD46 domain that carries two sequential proline residues (PP motif) and penetrates deeply into a hydrophobic socket in MV-H. We identify a similar PP motif in SLAM, defining a common measles virus recognition epitope in the CD46 and SLAM receptor proteins. Structure of the measles virus hemagglutinin bound to the CD46 receptor.,Santiago C, Celma ML, Stehle T, Casasnovas JM Nat Struct Mol Biol. 2010 Jan;17(1):124-9. Epub 2009 Dec 13. PMID:20010840[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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