2zb5

Crystal structure of the measles virus hemagglutinin (complex-sugar-type)

spinqualitylabelsall models 2zb5, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2zb5 is a 1 chain structure with sequence from Measles virus strain Edmonston-B. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3Å Ligands: NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HEMA_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. Publication Abstract from PubMed Measles still remains a major cause of childhood morbidity and mortality worldwide. Measles virus (MV) vaccines are highly successful, but the mechanism underlying their efficacy has been unclear. Here we report the crystal structure of the MV attachment protein, hemagglutinin, responsible for MV entry. The receptor-binding head domain exhibits a cubic-shaped beta-propeller structure and forms a homodimer. N-linked sugars appear to mask the broad regions and cause the two molecules forming the dimer to tilt oppositely toward the horizontal plane. Accordingly, residues of the putative receptor-binding site, highly conserved among MV strains, are strategically positioned in the unshielded area of the protein. These conserved residues also serve as epitopes for neutralizing antibodies, ensuring the serological monotype, a basis for effective MV vaccines. Our findings suggest that sugar moieties in the MV hemagglutinin critically modulate virus-receptor interaction as well as antiviral antibody responses, differently from sugars of the HIV gp120, which allow for immune evasion. Crystal structure of measles virus hemagglutinin provides insight into effective vaccines.,Hashiguchi T, Kajikawa M, Maita N, Takeda M, Kuroki K, Sasaki K, Kohda D, Yanagi Y, Maenaka K Proc Natl Acad Sci U S A. 2007 Dec 4;104(49):19535-40. Epub 2007 Nov 14. PMID:18003910 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Hemagglutinin 3D structures

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