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Structure of the tetramerization domain of measles virus phosphoprotein
Guillaume Communie1, Thibaut Crépin, Damien Maurin
1UJF-EMBL-CNRS, UMI 3265, Unit for Virus Host Cell Interactions, Grenoble, France.
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.
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