Structural Basis for RNA Binding and Homo-Oligomer Formation by Influenza B Virus Nucleoprotein
Publication in refereed journal


摘要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.
著者Ng AKL, Lam MKH, Zhang HM, Liu JH, Au SWN, Chan PKS, Wang JH, Shaw PC
期刊名稱Journal of Virology
出版社American Society for Microbiology
頁次6758 - 6767
Web of Science 學科類別Virology; VIROLOGY

上次更新時間 2020-06-08 於 02:34