View source for 7nfq


==Fujian capmidlink domain in complex with Nb8193==
<StructureSection load='7nfq' size='340' side='right'caption='[[7nfq]], [[Resolution|resolution]] 1.68&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7nfq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Camelidae_mixed_library Camelidae mixed library] and [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/duck/Fujian/13/2002(H5N1)) Influenza A virus (A/duck/Fujian/13/2002(H5N1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NFQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NFQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.68&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7nfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nfq OCA], [https://pdbe.org/7nfq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nfq RCSB], [https://www.ebi.ac.uk/pdbsum/7nfq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nfq ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Influenza A viruses cause seasonal epidemics and global pandemics, representing a considerable burden to healthcare systems. Central to the replication cycle of influenza viruses is the viral RNA-dependent RNA polymerase which transcribes and replicates the viral RNA genome. The polymerase undergoes conformational rearrangements and interacts with viral and host proteins to perform these functions. Here we determine the structure of the 1918 influenza virus polymerase in transcriptase and replicase conformations using cryo-electron microscopy (cryo-EM). We then structurally and functionally characterise the binding of single-domain nanobodies to the polymerase of the 1918 pandemic influenza virus. Combining these functional and structural data we identify five sites on the polymerase which are sensitive to inhibition by nanobodies. We propose that the binding of nanobodies at these sites either prevents the polymerase from assuming particular functional conformations or interactions with viral or host factors. The polymerase is highly conserved across the influenza A subtypes, suggesting these sites as effective targets for potential influenza antiviral development.

Mapping inhibitory sites on the RNA polymerase of the 1918 pandemic influenza virus using nanobodies.,Keown JR, Zhu Z, Carrique L, Fan H, Walker AP, Serna Martin I, Pardon E, Steyaert J, Fodor E, Grimes JM Nat Commun. 2022 Jan 11;13(1):251. doi: 10.1038/s41467-021-27950-w. PMID:35017564<ref>PMID:35017564</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7nfq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Camelidae mixed library]]
[[Category: Large Structures]]
[[Category: Fodor E]]
[[Category: Grimes JM]]
[[Category: Keown JR]]