3INB
Structure of the measles virus hemagglutinin bound to the CD46 receptor
Summary for 3INB
| Entry DOI | 10.2210/pdb3inb/pdb |
| Related | 1CKL 2O39 2RKC 2ZB5 2ZB6 |
| Descriptor | Hemagglutinin glycoprotein, Membrane cofactor protein, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | measles, beta propeller, envelope protein, hemagglutinin, viral protein. membrane cofactor protein, mcp, cd46, virus receptor complex, scr, complement control protein, immune system complex, membrane, transmembrane, virion, cell membrane, glycoprotein, host-virus interaction, signal-anchor, complement pathway, disease mutation, disulfide bond, fertilization, immune response, innate immunity, phosphoprotein, sushi, viral protein, immune system, viral protein-immune system complex, viral protein/immune system |
| Biological source | Measles virus strain Edmonston (viruses) More |
| Cellular location | Virion membrane; Single-pass type II membrane protein (Potential): P08362 Cytoplasmic vesicle, secretory vesicle, acrosome inner membrane; Single-pass type I membrane protein: P15529 |
| Total number of polymer chains | 4 |
| Total formula weight | 133770.06 |
| Authors | Santiago, C.,Celma, M.L.,Stehle, T.,Casasnovas, J.M. (deposition date: 2009-08-12, release date: 2009-12-22, Last modification date: 2024-11-20) |
| Primary citation | Santiago, C.,Celma, M.L.,Stehle, T.,Casasnovas, J.M. Structure of the measles virus hemagglutinin bound to the CD46 receptor Nat.Struct.Mol.Biol., 17:124-129, 2010 Cited by PubMed Abstract: The 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. PubMed: 20010840DOI: 10.1038/nsmb.1726 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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