Hogle J M, Chow M, Filman D J
Science. 1985 Sep 27;229(4720):1358-65. doi: 10.1126/science.2994218.
The three-dimensional structure of poliovirus has been determined at 2.9 A resolution by x-ray crystallographic methods. Each of the three major capsid proteins (VP1, VP2, and VP3) contains a "core" consisting of an eight-stranded antiparallel beta barrel with two flanking helices. The arrangement of beta strands and helices is structurally similar and topologically identical to the folding pattern of the capsid proteins of several icosahedral plant viruses. In each of the major capsid proteins, the "connecting loops" and NH2- and COOH-terminal extensions are structurally dissimilar. The packing of the subunit "cores" to form the virion shell is reminiscent of the packing in the T = 3 plant viruses, but is significantly different in detail. Differences in the orientations of the subunits cause dissimilar contacts at protein-protein interfaces, and are also responsible for two major surface features of the poliovirion: prominent peaks at the fivefold and threefold axes of the particle. The positions and interactions of the NH2- and COOH-terminal strands of the capsid proteins have important implications for virion assembly. Several of the "connecting loops" and COOH-terminal strands form prominent radial projections which are the antigenic sites of the virion.
通过X射线晶体学方法已确定脊髓灰质炎病毒的三维结构，分辨率为2.9埃。三种主要衣壳蛋白（VP1、VP2和VP3）中的每一种都包含一个“核心”，该核心由一个带有两个侧翼螺旋的八链反平行β桶组成。β链和螺旋的排列在结构上相似，拓扑结构与几种二十面体植物病毒的衣壳蛋白折叠模式相同。在每种主要衣壳蛋白中，“连接环”以及NH2和COOH末端延伸在结构上是不同的。亚基“核心”堆积形成病毒粒子外壳的方式让人联想到T = 3植物病毒中的堆积方式，但在细节上有显著差异。亚基方向的差异导致蛋白质-蛋白质界面处的接触不同，也造成了脊髓灰质炎病毒粒子的两个主要表面特征：粒子五重轴和三重轴处的突出峰。衣壳蛋白的NH2和COOH末端链的位置及相互作用对病毒粒子组装具有重要意义。几个“连接环”和COOH末端链形成突出的径向突起，这些是病毒粒子的抗原位点。
