title: Structure of the tetramerization domain of measles virus phosphoprotein.
abstract: The atomic structure of the stable tetramerization domain of the measles virus phosphoprotein shows a tight four-stranded coiled coil. Although at first sight similar to the tetramerization domain of the Sendai virus phosphoprotein, which has a hydrophilic interface, the measles virus domain has kinked helices that have a strongly hydrophobic interface and it lacks the additional N-terminal three helical bundles linking the long helices.
authors.affiliation: UJF-EMBL-CNRS, UMI 3265, Unit for Virus Host Cell Interactions, Grenoble, France.
authors.forename: Guillaume
authors.initials: G
authors.lastname: Communie
authors.forename: Thibaut
authors.initials: T
authors.lastname: Crépin
authors.forename: Damien
authors.initials: D
authors.lastname: Maurin
authors.forename: Malene Ringkjøbing
authors.initials: MR
authors.lastname: Jensen
authors.forename: Martin
authors.initials: M
authors.lastname: Blackledge
authors.forename: Rob W H
authors.initials: RW
authors.lastname: Ruigrok
mesh_terms: D009682:Magnetic Resonance Spectroscopy; D008459:Measles virus / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010750:Phosphoproteins / Q000737:chemistry*; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D014764:Viral Proteins / Q000737:chemistry*
chemical_list: D010750:Phosphoproteins; D014764:Viral Proteins