STRUCTURE OF SIMIAN VIRUS-40 AT 3.8-A RESOLUTION
STRUCTURE OF SIMIAN VIRUS-40 AT 3.8-A RESOLUTION
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DOI：
10.1038/354278a0
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发表时间：
1991-11-28
期刊：
影响因子：
64.8
通讯作者：
HARRISON, SC
中科院分区：
文献类型：
--
作者：
LIDDINGTON, RC;YAN, Y;HARRISON, SC
猴病毒40的晶体学结构表明，形成外壳的病毒蛋白VP 1的72个五聚体具有相同的构象，除了它们的亚基的C-末端臂。五个臂从每个五聚体中出现并插入相邻的五聚体中。这种将标准构建块捆绑在一起的做法允许在不牺牲特异性的情况下实现填充几何形状的所需可变性。
The crystallographically determined structure of simian virus 40 shows that the 72 pentamers of viral protein VP1, which form the outer shell, have identical conformations except for the C-terminal arms of their subunits. Five arms emerge from each pentamer and insert into neighbouring pentamers. This tying together of standard building blocks allows for the required variability in packing geometry without sacrificing specificity.