7od3: Difference between revisions
New page: '''Unreleased structure''' The entry 7od3 is ON HOLD Authors: Description: Category: Unreleased Structures |
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==SARS CoV-2 Spike protein, Bristol UK Deletion variant, Closed conformation, C3 symmetry== | |||
<StructureSection load='7od3' size='340' side='right'caption='[[7od3]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OD3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OD3 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]] 2.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EIC:LINOLEIC+ACID'>EIC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=7od3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7od3 OCA], [https://pdbe.org/7od3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7od3 RCSB], [https://www.ebi.ac.uk/pdbsum/7od3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7od3 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
As the global burden of SARS-CoV-2 infections escalates, so does the evolution of viral variants with increased transmissibility and pathology. In addition to this entrenched diversity, RNA viruses can also display genetic diversity within single infected hosts with co-existing viral variants evolving differently in distinct cell types. The BriSDelta variant, originally identified as a viral subpopulation from SARS-CoV-2 isolate hCoV-19/England/02/2020, comprises in the spike an eight amino-acid deletion encompassing a furin recognition motif and S1/S2 cleavage site. We elucidate the structure, function and molecular dynamics of this spike providing mechanistic insight into how the deletion correlates to viral cell tropism, ACE2 receptor binding and infectivity of this SARS-CoV-2 variant. Our results reveal long-range allosteric communication between functional domains that differ in the wild-type and the deletion variant and support a view of SARS-CoV-2 probing multiple evolutionary trajectories in distinct cell types within the same infected host. | |||
Structural insights in cell-type specific evolution of intra-host diversity by SARS-CoV-2.,Gupta K, Toelzer C, Williamson MK, Shoemark DK, Oliveira ASF, Matthews DA, Almuqrin A, Staufer O, Yadav SKN, Borucu U, Garzoni F, Fitzgerald D, Spatz J, Mulholland AJ, Davidson AD, Schaffitzel C, Berger I Nat Commun. 2022 Jan 11;13(1):222. doi: 10.1038/s41467-021-27881-6. PMID:35017512<ref>PMID:35017512</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7od3" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Spike protein 3D structures|Spike protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Berger I]] | |||
[[Category: Borucu U]] | |||
[[Category: Gupta K]] | |||
[[Category: Schaffitzel C]] | |||
[[Category: Toelzer C]] | |||
[[Category: Yadav SKN]] | |||
Latest revision as of 09:37, 21 November 2024
SARS CoV-2 Spike protein, Bristol UK Deletion variant, Closed conformation, C3 symmetrySARS CoV-2 Spike protein, Bristol UK Deletion variant, Closed conformation, C3 symmetry
Structural highlights
Publication Abstract from PubMedAs the global burden of SARS-CoV-2 infections escalates, so does the evolution of viral variants with increased transmissibility and pathology. In addition to this entrenched diversity, RNA viruses can also display genetic diversity within single infected hosts with co-existing viral variants evolving differently in distinct cell types. The BriSDelta variant, originally identified as a viral subpopulation from SARS-CoV-2 isolate hCoV-19/England/02/2020, comprises in the spike an eight amino-acid deletion encompassing a furin recognition motif and S1/S2 cleavage site. We elucidate the structure, function and molecular dynamics of this spike providing mechanistic insight into how the deletion correlates to viral cell tropism, ACE2 receptor binding and infectivity of this SARS-CoV-2 variant. Our results reveal long-range allosteric communication between functional domains that differ in the wild-type and the deletion variant and support a view of SARS-CoV-2 probing multiple evolutionary trajectories in distinct cell types within the same infected host. Structural insights in cell-type specific evolution of intra-host diversity by SARS-CoV-2.,Gupta K, Toelzer C, Williamson MK, Shoemark DK, Oliveira ASF, Matthews DA, Almuqrin A, Staufer O, Yadav SKN, Borucu U, Garzoni F, Fitzgerald D, Spatz J, Mulholland AJ, Davidson AD, Schaffitzel C, Berger I Nat Commun. 2022 Jan 11;13(1):222. doi: 10.1038/s41467-021-27881-6. PMID:35017512[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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