麻疹病毒磷蛋白四聚化结构域。
Structure of the tetramerization domain of measles virus phosphoprotein.
机构信息
UJF-EMBL-CNRS, UMI 3265, Unit for Virus Host Cell Interactions, Grenoble, France.
出版信息
J Virol. 2013 Jun;87(12):7166-9. doi: 10.1128/JVI.00487-13. Epub 2013 Apr 10.
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.
摘要
麻疹病毒磷酸蛋白稳定四聚化结构域的原子结构呈现出紧密的四股螺旋卷曲。尽管乍一看类似于具有亲水界面的仙台病毒磷酸蛋白的四聚化结构域，但麻疹病毒结构域的螺旋是扭曲的，具有强烈的疏水性界面，并且缺乏连接长螺旋的额外的 N 端三个螺旋束。
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