Structure of the tetramerization domain of measles virus phosphoprotein.
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ABSTRACT:
SUBMITTER: Communie G
PROVIDER: S-EPMC3676081 | biostudies-literature | 2013 Jun
REPOSITORIES: biostudies-literature
Publications
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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