Key result
The atomic structure of the measles virus phosphoprotein tetramerization domain reveals a tight four-stranded coiled coil with kinked helices and a strongly hydrophobic interface.
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No immediate clinical impact on measles care; leaves open structure-guided antiviral targeting of the coiled-coil interface.
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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Communie et al. (2013) studied this question. The atomic structure of the measles virus phosphoprotein tetramerization domain reveals a tight four-stranded coiled coil with kinked helices and a strongly hydrophobic interface.
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