2iqh: Difference between revisions

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|ACTIVITY=  
|ACTIVITY=  
|GENE= NP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11320 Influenza A virus])
|GENE= NP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11320 Influenza A virus])
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iqh OCA], [http://www.ebi.ac.uk/pdbsum/2iqh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2iqh RCSB]</span>
}}
}}


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[[Category: rna binding]]
[[Category: rna binding]]


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Revision as of 03:47, 31 March 2008

File:2iqh.jpg


PDB ID 2iqh

Drag the structure with the mouse to rotate
, resolution 3.20Å
Gene: NP (Influenza A virus)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Influenza A virus nucleoprotein NP at 3.2A resolution


OverviewOverview

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. Here we report a 3.2 A 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. 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.

About this StructureAbout this Structure

2IQH is a Single protein structure of sequence from Influenza a virus. Full crystallographic information is available from OCA.

ReferenceReference

The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA., Ye Q, Krug RM, Tao YJ, Nature. 2006 Dec 21;444(7122):1078-82. Epub 2006 Dec 6. PMID:17151603

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