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在8.5埃分辨率下观察到疱疹病毒衣壳。

Seeing the herpesvirus capsid at 8.5 A.

作者信息

Zhou Z H, Dougherty M, Jakana J, He J, Rixon F J, Chiu W

机构信息

Department of Pathology and Laboratory Medicine, University of Texas-Houston Medical School, Houston, TX 77030, USA.

出版信息

Science. 2000 May 5;288(5467):877-80. doi: 10.1126/science.288.5467.877.

Abstract

Human herpesviruses are large and structurally complex viruses that cause a variety of diseases. The three-dimensional structure of the herpesvirus capsid has been determined at 8.5 angstrom resolution by electron cryomicroscopy. More than 30 putative alpha helices were identified in the four proteins that make up the 0.2 billion-dalton shell. Some of these helices are located at domains that undergo conformational changes during capsid assembly and DNA packaging. The unique spatial arrangement of the heterotrimer at the local threefold positions accounts for the asymmetric interactions with adjacent capsid components and the unusual co-dependent folding of its subunits.

摘要

人类疱疹病毒是大型且结构复杂的病毒,可引发多种疾病。疱疹病毒衣壳的三维结构已通过电子冷冻显微镜以8.5埃的分辨率确定。在构成20亿道尔顿外壳的四种蛋白质中鉴定出了30多个假定的α螺旋。其中一些螺旋位于衣壳组装和DNA包装过程中发生构象变化的结构域。异源三聚体在局部三重位置的独特空间排列解释了其与相邻衣壳成分的不对称相互作用及其亚基不同寻常的共同依赖折叠。

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