4.6 Article

Structural Basis for RNA Binding and Homo-Oligomer Formation by Influenza B Virus Nucleoprotein

期刊

JOURNAL OF VIROLOGY
卷 86, 期 12, 页码 6758-6767

出版社

AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.00073-12

关键词

-

类别

资金

  1. Research Grants Council of Hong Kong [CUHK473810]
  2. Claudia Adams Barr Program in Cancer Research
  3. University Grants Council of Hong Kong [SEG CUHK08]

向作者/读者索取更多资源

Influenza virus nucleoprotein (NP) is the major component of the viral ribonucleoprotein complex, which is crucial for the transcription and replication of the viral genome. We have determined the crystal structure of influenza B virus NP to a resolution of 3.2 angstrom. Influenza B NP contains a head, a body domain, and a tail loop. The electropositive groove between the head and body domains of influenza B NP is crucial for RNA binding. This groove also contains an extended flexible charged loop (amino acids [aa] 125 to 149), and two lysine clusters at the first half of this loop were shown to be crucial for binding RNA. Influenza B virus NP forms a crystallographic homotetramer by inserting the tail loop into the body domain of the neighboring NP molecule. A deeply buried salt bridge between R472 and E395 and a hydrophobic cluster at F468 are the major driving forces for the insertion. The analysis of the influenza B virus NP structure and function and comparisons with influenza A virus NP provide insights into the mechanisms of action and underpin efforts to design inhibitors for this class of proteins.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.6
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据