Roberts M M, White J L, Grütter M G, Burnett R M
Science. 1986 May 30;232(4754):1148-51. doi: 10.1126/science.3704642.
The three-dimensional crystal structure of the adenovirus major coat protein is presented. Adenovirus type 2 hexon, at 967 residues, is now the longest polypeptide whose structure has been determined crystallographically. Taken with our model for hexon packing, which positions the 240 trimeric hexons in the capsid, the structure defines 60% of the protein within the 150 X 10(6) dalton virion. The assembly provides the first details of a DNA-containing animal virus that is 20 times larger than the spherical RNA viruses previously described. Unexpectedly, the hexon subunit contains two similar beta-barrels whose topology is identical to those of the spherical RNA viruses, but whose architectural role in adenovirus is very different. The hexon structure reveals several distinctive features related to its function as a stable protective coat, and shows that the type-specific immunological determinants are restricted to the virion surface.
本文展示了腺病毒主要衣壳蛋白的三维晶体结构。2型腺病毒六邻体由967个氨基酸残基组成，是目前已通过晶体学确定结构的最长多肽。结合我们的六邻体包装模型（该模型确定了衣壳中240个三聚体六邻体的位置），该结构定义了150×10⁶道尔顿病毒粒子中60%的蛋白质。这种组装首次提供了一种含DNA动物病毒的详细信息，该病毒比之前描述的球形RNA病毒大20倍。出乎意料的是，六邻体亚基包含两个相似的β桶结构，其拓扑结构与球形RNA病毒的相同，但在腺病毒中的结构作用却大不相同。六邻体结构揭示了与其作为稳定保护衣功能相关的几个独特特征，并表明型特异性免疫决定簇仅限于病毒粒子表面。
