• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Nature >The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA
【24h】

The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA

机译：甲型流感病毒核蛋白形成寡聚体并结合RNA的机制

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

Influenza A viruses pose a serious threat to world public health, particularly the currently circulating avian H5N1 viruses. The influenza viral nucleoprotein forms the protein scaffold of the helical genomic ribonucleoprotein complexes, and has a critical role in viral RNA replication(1). Here we report a 3.2 angstrom crystal structure of this nucleoprotein, the overall shape of which resembles a crescent with a head and a body domain, with a protein fold different compared with that of the rhabdovirus nucleoprotein(2,3). Oligomerization of the influenza virus nucleoprotein is mediated by a flexible tail loop that is inserted inside a neighbouring molecule. This flexibility in the tail loop enables the nucleoprotein to form loose polymers as well as rigid helices, both of which are important for nucleoprotein functions. Single residue mutations in the tail loop result in the complete loss of nucleoprotein oligomerization. An RNA-binding groove, which is found between the head and body domains at the exterior of the nucleoprotein oligomer, is lined with highly conserved basic residues widely distributed in the primary sequence. The nucleoprotein structure shows that only one of two proposed nuclear localization signals are accessible, and suggests that the body domain of nucleoprotein contains the binding site for the viral polymerase. Our results identify the tail loop binding pocket as a potential target for antiviral development.
机译：甲型流感病毒严重威胁着世界公共卫生，特别是目前正在传播的禽类H5N1病毒。流感病毒核蛋白形成螺旋基因组核糖核蛋白复合物的蛋白支架，并且在病毒RNA复制中起关键作用（1）。在这里，我们报道了这种核蛋白的3.2埃晶体结构，其总体形状类似于带有头部和体域的月牙形，与弹状病毒核蛋白相比其蛋白质折叠倍数不同（2,3）。流感病毒核蛋白的寡聚是通过插入相邻分子内部的柔性尾环介导的。尾环的这种灵活性使核蛋白能够形成疏松的聚合物以及刚性螺旋，这两者对于核蛋白的功能都很重要。尾环中的单个残基突变导致核蛋白寡聚完全丧失。 RNA结合沟位于核蛋白寡聚物外部的头部和身体结构域之间，内衬有高度保守的基本残基，这些残基广泛分布于一级序列中。核蛋白结构显示只有两个拟议的核定位信号之一可访问，并且表明核蛋白的体域包含病毒聚合酶的结合位点。我们的结果确定了尾环结合口袋是抗病毒发展的潜在目标。

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