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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.

SUBMITTER: Communie G 

PROVIDER: S-EPMC3676081 | biostudies-literature | 2013 Jun

REPOSITORIES: biostudies-literature

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Structure of the tetramerization domain of measles virus phosphoprotein.

Communie Guillaume G   Crépin Thibaut T   Maurin Damien D   Jensen Malene Ringkjøbing MR   Blackledge Martin M   Ruigrok Rob W H RW  

Journal of virology 20130410 12

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. ...[more]

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