3-DIMENSIONAL STRUCTURE OF POLIOVIRUS AT 2.9 A RESOLUTION
3-DIMENSIONAL STRUCTURE OF POLIOVIRUS AT 2.9 A RESOLUTION
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DOI：
10.1126/science.2994218
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发表时间：
1985-01-01
期刊：
影响因子：
56.9
通讯作者：
FILMAN, DJ
中科院分区：
文献类型：
--
作者：
HOGLE, JM;CHOW, M;FILMAN, DJ
脊髓灰质炎病毒的三维结构已通过X射线晶体学方法在2.9 nm分辨率下确定。三种主要衣壳蛋白（VP 1、VP 2和VP 3）中的每一种都含有一个由八链反平行β桶组成的“核心”，该桶具有两个侧翼螺旋。β链和螺旋的排列与几种二十面体植物病毒衣壳蛋白的折叠模式在结构上相似且拓扑学上相同。在每个主要衣壳蛋白中，“连接环”和NH 2-和COOH-末端延伸在结构上是不同的。亚基“核心”的包装形成病毒体外壳，这让人想起T = 3植物病毒的包装，但在细节上有显著不同。亚基方向的差异导致蛋白质-蛋白质界面处的不同接触，并且还负责脊髓灰质炎病毒的两个主要表面特征：颗粒的五倍和三倍轴处的突出峰。衣壳蛋白的NH 2-和COOH-末端链的位置和相互作用对病毒体组装具有重要意义。几个“连接环”和COOH末端链形成突出的放射状突起，这些突起是病毒粒子的抗原位点。
The three-dimensional structure of poliovirus has been determined at 2.9 Å 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 theT= 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.