UVHCI, UMI 3265 UJF-EMBL-CNRS, BP 181, 38042 Grenoble, Cedex 9, France.
J Virol. 2010 Apr;84(7):3707-10. doi: 10.1128/JVI.02557-09. Epub 2010 Jan 20.
The crystal structure of the dimerization domain of rabies virus phosphoprotein was determined. The monomer consists of two alpha-helices that make a helical hairpin held together mainly by hydrophobic interactions. The monomer has a hydrophilic and a hydrophobic face, and in the dimer two monomers pack together through their hydrophobic surfaces. This structure is very different from the dimerization domain of the vesicular stomatitis virus phosphoprotein and also from the tetramerization domain of the Sendai virus phosphoprotein, suggesting that oligomerization is conserved but not structure.
狂犬病病毒磷蛋白二聚化结构域的晶体结构已被确定。单体由两个α螺旋组成,形成一个主要由疏水相互作用保持的发夹结构。单体具有亲水和疏水两个面,在二聚体中,两个单体通过疏水表面结合在一起。这种结构与水疱性口炎病毒磷蛋白的二聚化结构域以及仙台病毒磷蛋白的四聚化结构域非常不同,表明寡聚化是保守的,但结构不是。