Structure of the tetramerization domain of measles virus phosphoprotein.

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Communie, Guillaume | Crépin, Thibaut | Maurin, Damien | Jensen, Malene Ringkjøbing | Blackledge, Martin | Ruigrok, Rob W H

Edité par CCSD ; American Society for Microbiology -

International audience. 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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