Structural highlights
Publication Abstract from PubMed
The atomic structure of the stable tetramerization domain of the measles virus phosphoprotein shows a tight four-stranded coiled coil. Although at first look similar to the tetramerization domain of the Sendai virus phosphoprotein that 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.
Structure of the Tetramerization Domain of Measles Virus Phosphoprotein.,Communie G, Crepin T, Maurin D, Ringkjobing Jensen M, Blackledge M, Ruigrok RW J Virol. 2013 Apr 10. PMID:23576502[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Communie G, Crepin T, Maurin D, Ringkjobing Jensen M, Blackledge M, Ruigrok RW. Structure of the Tetramerization Domain of Measles Virus Phosphoprotein. J Virol. 2013 Apr 10. PMID:23576502 doi:10.1128/JVI.00487-13
