衣壳
帽状体
外壳蛋白
核糖核酸
病毒学
生物
乳腺腺病毒
蛋白质亚单位
结构蛋白
物理
病毒
腺病毒科
结晶学
化学
遗传学
基因
重组DNA
作者
Michael M. Roberts,Janice L. White,Markus G. Grütter,Roger M. Burnett
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:1986-05-30
卷期号:232 (4754): 1148-1151
被引量:245
标识
DOI:10.1126/science.3704642
摘要
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 × 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 β-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.
科研通智能强力驱动
Strongly Powered by AbleSci AI