8r1j: Difference between revisions
New page: '''Unreleased structure''' The entry 8r1j is ON HOLD Authors: Description: Category: Unreleased Structures |
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==Structure of avian H5N1 influenza A polymerase dimer in complex with human ANP32B.== | |||
<StructureSection load='8r1j' size='340' side='right'caption='[[8r1j]], [[Resolution|resolution]] 3.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8r1j]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Influenza_A_virus Influenza A virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8R1J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8R1J FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.2Å</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=8r1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8r1j OCA], [https://pdbe.org/8r1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8r1j RCSB], [https://www.ebi.ac.uk/pdbsum/8r1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8r1j ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A5Z236_9INFA A5Z236_9INFA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Avian influenza A viruses (IAVs) pose a public health threat, as they are capable of triggering pandemics by crossing species barriers. Replication of avian IAVs in mammalian cells is hindered by species-specific variation in acidic nuclear phosphoprotein 32 (ANP32) proteins, which are essential for viral RNA genome replication. Adaptive mutations enable the IAV RNA polymerase (FluPolA) to surmount this barrier. Here, we present cryo-electron microscopy structures of monomeric and dimeric avian H5N1 FluPolA with human ANP32B. ANP32B interacts with the PA subunit of FluPolA in the monomeric form, at the site used for its docking onto the C-terminal domain of host RNA polymerase II during viral transcription. ANP32B acts as a chaperone, guiding FluPolA towards a ribonucleoprotein-associated FluPolA to form an asymmetric dimer-the replication platform for the viral genome. These findings offer insights into the molecular mechanisms governing IAV genome replication, while enhancing our understanding of the molecular processes underpinning mammalian adaptations in avian-origin FluPolA. | |||
Structures of H5N1 influenza polymerase with ANP32B reveal mechanisms of genome replication and host adaptation.,Staller E, Carrique L, Swann OC, Fan H, Keown JR, Sheppard CM, Barclay WS, Grimes JM, Fodor E Nat Commun. 2024 May 15;15(1):4123. doi: 10.1038/s41467-024-48470-3. PMID:38750014<ref>PMID:38750014</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8r1j" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Influenza A virus]] | |||
[[Category: Large Structures]] | |||
[[Category: Carrique L]] | |||
[[Category: Fan H]] | |||
[[Category: Fodor E]] | |||
[[Category: Grimes JM]] | |||
[[Category: Keown JR]] | |||
[[Category: Staller E]] | |||
Latest revision as of 22:56, 29 May 2024
Structure of avian H5N1 influenza A polymerase dimer in complex with human ANP32B.Structure of avian H5N1 influenza A polymerase dimer in complex with human ANP32B.
Structural highlights
FunctionPublication Abstract from PubMedAvian influenza A viruses (IAVs) pose a public health threat, as they are capable of triggering pandemics by crossing species barriers. Replication of avian IAVs in mammalian cells is hindered by species-specific variation in acidic nuclear phosphoprotein 32 (ANP32) proteins, which are essential for viral RNA genome replication. Adaptive mutations enable the IAV RNA polymerase (FluPolA) to surmount this barrier. Here, we present cryo-electron microscopy structures of monomeric and dimeric avian H5N1 FluPolA with human ANP32B. ANP32B interacts with the PA subunit of FluPolA in the monomeric form, at the site used for its docking onto the C-terminal domain of host RNA polymerase II during viral transcription. ANP32B acts as a chaperone, guiding FluPolA towards a ribonucleoprotein-associated FluPolA to form an asymmetric dimer-the replication platform for the viral genome. These findings offer insights into the molecular mechanisms governing IAV genome replication, while enhancing our understanding of the molecular processes underpinning mammalian adaptations in avian-origin FluPolA. Structures of H5N1 influenza polymerase with ANP32B reveal mechanisms of genome replication and host adaptation.,Staller E, Carrique L, Swann OC, Fan H, Keown JR, Sheppard CM, Barclay WS, Grimes JM, Fodor E Nat Commun. 2024 May 15;15(1):4123. doi: 10.1038/s41467-024-48470-3. PMID:38750014[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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