3ALZ
Crystal structure of the measles virus hemagglutinin bound to its cellular receptor SLAM (Form I)
Summary for 3ALZ
| Entry DOI | 10.2210/pdb3alz/pdb |
| Related | 3ALW 3ALX |
| Descriptor | Hemagglutinin, CDw150, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
| Functional Keywords | viral protein-receptor complex, six-bladed beta-propeller fold, immunoglobulin fold, beta-sandwich, viral protein-membrane protein complex, viral protein/membrane protein |
| Biological source | Measles virus More |
| Total number of polymer chains | 2 |
| Total formula weight | 71112.01 |
| Authors | Hashiguchi, T.,Ose, T.,Kubota, M.,Maita, N.,Kamishikiryo, J.,Maenaka, K.,Yanagi, Y. (deposition date: 2010-08-11, release date: 2011-01-12, Last modification date: 2024-10-23) |
| Primary citation | Hashiguchi, T.,Ose, T.,Kubota, M.,Maita, N.,Kamishikiryo, J.,Maenaka, K.,Yanagi, Y. Structure of the measles virus hemagglutinin bound to its cellular receptor SLAM Nat.Struct.Mol.Biol., 18:135-141, 2011 Cited by PubMed Abstract: Measles virus, a major cause of childhood morbidity and mortality worldwide, predominantly infects immune cells using signaling lymphocyte activation molecule (SLAM) as a cellular receptor. Here we present crystal structures of measles virus hemagglutinin (MV-H), the receptor-binding glycoprotein, in complex with SLAM. The MV-H head domain binds to a β-sheet of the membrane-distal ectodomain of SLAM using the side of its β-propeller fold. This is distinct from attachment proteins of other paramyxoviruses that bind receptors using the top of their β-propeller. The structure provides templates for antiviral drug design, an explanation for the effectiveness of the measles virus vaccine, and a model of the homophilic SLAM-SLAM interaction involved in immune modulations. Notably, the crystal structures obtained show two forms of the MV-H-SLAM tetrameric assembly (dimer of dimers), which may have implications for the mechanism of fusion triggering. PubMed: 21217702DOI: 10.1038/nsmb.1969 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4.515 Å) |
Structure validation
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