2iqh
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(New page: 200px<br /><applet load="2iqh" size="350" color="white" frame="true" align="right" spinBox="true" caption="2iqh, resolution 3.20Å" /> '''Influenza A virus nu...)
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Revision as of 18:45, 29 January 2008
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Influenza A virus nucleoprotein NP at 3.2A resolution
Overview
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 Structure
2IQH is a Single protein structure of sequence from Influenza a virus. Full crystallographic information is available from OCA.
Reference
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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