tetano
Editor, Senior Moderator
J Virol. 2012 Apr 11. [Epub ahead of print]
Structural basis for RNA-binding and homo-oligomer formation by influenza B virus nucleoprotein.
Ng AK, Lam MK, Zhang H, Liu J, Au SW, Chan PK, Wang J, Shaw PC.
Source
Centre for Protein Science and Crystallography, School of Life Sciences, The Chinese University of Hong Kong, Shatin, Hong Kong, China.
Abstract
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 ?. 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 (aa. 125-149) and two lysine clusters at the first half of this loop were shown to be crucial for binding RNA. Influenza B NP forms a crystallographic homo-tetramer by inserting the tail loop into the body domain of the neighboring NP molecule. A deeply buried salt bridge R472-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.
PMID:
22496219
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/22496219
Structural basis for RNA-binding and homo-oligomer formation by influenza B virus nucleoprotein.
Ng AK, Lam MK, Zhang H, Liu J, Au SW, Chan PK, Wang J, Shaw PC.
Source
Centre for Protein Science and Crystallography, School of Life Sciences, The Chinese University of Hong Kong, Shatin, Hong Kong, China.
Abstract
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 ?. 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 (aa. 125-149) and two lysine clusters at the first half of this loop were shown to be crucial for binding RNA. Influenza B NP forms a crystallographic homo-tetramer by inserting the tail loop into the body domain of the neighboring NP molecule. A deeply buried salt bridge R472-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.
PMID:
22496219
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/22496219