File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Structural basis for RNA binding and homo-oligomer formation by influenza B virus nucleoprotein

TitleStructural basis for RNA binding and homo-oligomer formation by influenza B virus nucleoprotein
Authors
Issue Date2012
PublisherAmerican Society for Microbiology. The Journal's web site is located at http://jvi.asm.org/
Citation
Journal of Virology, 2012, v. 86 n. 12, p. 6758-6767 How to Cite?
AbstractInfluenza 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 A. 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.
Persistent Identifierhttp://hdl.handle.net/10722/152814
ISSN
2023 Impact Factor: 4.0
2023 SCImago Journal Rankings: 1.378
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorNg, AKL-
dc.contributor.authorLam, MKH-
dc.contributor.authorZhang, H-
dc.contributor.authorLiu, J-
dc.contributor.authorAu, SWN-
dc.contributor.authorChan, PKS-
dc.contributor.authorWang, J-
dc.contributor.authorShaw, PC-
dc.date.accessioned2012-07-16T09:49:24Z-
dc.date.available2012-07-16T09:49:24Z-
dc.date.issued2012-
dc.identifier.citationJournal of Virology, 2012, v. 86 n. 12, p. 6758-6767-
dc.identifier.issn0022-538X-
dc.identifier.urihttp://hdl.handle.net/10722/152814-
dc.description.abstractInfluenza 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 A. 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.-
dc.languageeng-
dc.publisherAmerican Society for Microbiology. The Journal's web site is located at http://jvi.asm.org/-
dc.relation.ispartofJournal of Virology-
dc.titleStructural basis for RNA binding and homo-oligomer formation by influenza B virus nucleoprotein-
dc.typeArticle-
dc.identifier.emailZhang, H: hzhang20@hku.hk-
dc.identifier.authorityZhang, H=rp00306-
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1128/JVI.00073-12-
dc.identifier.pmid22496219-
dc.identifier.pmcidPMC3393550-
dc.identifier.scopuseid_2-s2.0-84864007807-
dc.identifier.hkuros200471-
dc.identifier.volume86-
dc.identifier.issue12-
dc.identifier.spage6758-
dc.identifier.epage6767-
dc.identifier.isiWOS:000304894100035-
dc.publisher.placeUnited States-
dc.identifier.issnl0022-538X-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats