Interaction of polyomavirus internal protein VP2 with the major capsid protein VP1 and implications for participation of VP2 in viral entry
Interaction of polyomavirus internal protein VP2 with the major capsid protein VP1 and implications for participation of VP2 in viral entry
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DOI：
10.1093/emboj/17.12.3233
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发表时间：
1998-06-15
期刊：
影响因子：
11.4
通讯作者：
Harrison, SC
中科院分区：
文献类型：
--
作者：
Chen, XJS;Stehle, T;Harrison, SC
通过在大肠杆菌中共表达，制备了多瘤病毒内部蛋白VP2/VP3与五聚体主要衣壳蛋白VP1的复合物。VP2/VP3的C末端片段对于紧密结合是必需的，并且已确定了该片段与VP1五聚体复合的晶体结构，分辨率为2.2埃。该结构显示内部蛋白的单个拷贝与VP1五聚体之间存在特定的接触。在先前描述的病毒体结构中未检测到这些相互作用，但重组复合物中VP2的位置与病毒体电子密度图中的特征一致。VP2/VP3的C末端以一种不寻常的发夹样方式插入VP1五聚体的轴向腔中，在那里它通过疏水相互作用牢固锚定。内部蛋白的其余部分似乎具有显著的柔性。这种结构限制了病毒进入过程中内部蛋白暴露的可能模型。
A complex of the polyomavirus internal protein VP2/VP3 with the pentameric major capsid protein VPI has been prepared by co-expression in Escherichia coli, A C-terminal segment of VP2/VP3 is required for tight association, and a crystal structure of this segment, complexed with a VPI pentamer, has been determined at 2,2;Angstrom resolution. The structure shows specific contacts between a single copy of the internal protein and a pentamer of VP1, These interactions were not detected in the previously described structure of the virion, but the location of VP2 in the recombinant complex is consistent with features in the virion electron-density map. The C-terminus of VP2/VP3 inserts in an unusual, hairpin-like manner into the axial cavity of the VP1 pentamer, where it is anchored strongly by hydrophobic interactions, The remainder of the internal protein appears to have significant flexibility. This structure restricts possible models for exposure of the internal proteins during viral entry.