3ALX: Crystal Structure Of The Measles Virus Hemagglutinin Bound To Its Cellular Receptor Slam (mv-h(l482r)-slam(n102h/r108y) Fusion)

Citation:
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 beta-sheet of the membrane-distal ectodomain of SLAM using the side of its beta-propeller fold. This is distinct from attachment proteins of other paramyxoviruses that bind receptors using the top of their beta-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.
PDB ID: 3ALXDownload
MMDB ID: 87811
PDB Deposition Date: 2010/8/9
Updated in MMDB: 2017/06
Experimental Method:
x-ray diffraction
Resolution: 3.15  Å
Similar Structures:
Biological Unit for 3ALX: tetrameric; determined by author and by software (PISA)
Molecular Components in 3ALX
Label Count Molecule
Proteins (4 molecules)
4
Hemagglutinin,linker,cdw150
Molecule annotation
Chemicals (6 molecules)
1
6
* Click molecule labels to explore molecular sequence information.

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