Journal
JOURNAL OF VIROLOGY
Volume 87, Issue 12, Pages 7166-7169Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.00487-13
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Funding
- French Agence Nationale de la Recherche through the ANR SIMI7 ComplexDynamics
- French Agence Nationale de la Recherche through ANR MALZ TAUSTRUCT
- French Agence Nationale de la Recherche through ANR JCJC ProteinDisorder
- Finovi Foundation of Lyon
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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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