• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >Structure of the coat protein-binding domain of the scaffolding protein from a double-stranded DNA virus.
【24h】

Structure of the coat protein-binding domain of the scaffolding protein from a double-stranded DNA virus.

机译：来自双链DNA病毒的支架蛋白的外壳蛋白结合结构域的结构。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Scaffolding proteins are required for high fidelity assembly of most high T number dsDNA viruses such as the large bacteriophages, and the herpesvirus family. They function by transiently binding and positioning the coat protein subunits during capsid assembly. In both bacteriophage P22 and the herpesviruses the extreme scaffold C terminus is highly charged, is predicted to be an amphipathic alpha-helix, and is sufficient to bind the coat protein, suggesting a common mode of action. NMR studies show that the coat protein-binding domain of P22 scaffolding protein exhibits a helix-loop-helix motif stabilized by a hydrophobic core. One face of the motif is characterized by a high density of positive charges that could interact with the coat protein through electrostatic interactions. Results from previous studies with a truncation fragment and the observed salt sensitivity of the assembly process are explained by the NMR structure. Copyright 2000 Academic Press.
机译：支架蛋白是大多数高T数dsDNA病毒（例如大型噬菌体和疱疹病毒家族）的高保真装配所必需的。它们通过在衣壳装配过程中瞬时结合和定位外壳蛋白亚基而发挥作用。在噬菌体P22和疱疹病毒中，极端支架C末端均带高电荷，被认为是两亲性的α-螺旋，足以结合外壳蛋白，表明是一种常见的作用方式。 NMR研究表明，P22支架蛋白的外壳蛋白结合域显示出由疏水核稳定的螺旋-环-螺旋基序。图案的一个面的特征是高密度的正电荷，可以通过静电相互作用与外壳蛋白相互作用。 NMR结构解释了先前关于截短片段的研究结果以及组装过程中观察到的盐敏感性。版权所有2000学术出版社。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号