7ke4: Difference between revisions
New page: '''Unreleased structure''' The entry 7ke4 is ON HOLD Authors: Gobeil, S., Acharya, P. Description: SARS-CoV-2 D614G 3 RBD down Spike Protein Trimer without the P986-P987 stabilizing mu... |
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The | ==SARS-CoV-2 D614G 3 RBD down Spike Protein Trimer without the P986-P987 stabilizing mutations (S-GSAS-D614G Sub-class)== | ||
<StructureSection load='7ke4' size='340' side='right'caption='[[7ke4]], [[Resolution|resolution]] 3.21Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KE4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KE4 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]] 3.21Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=7ke4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ke4 OCA], [https://pdbe.org/7ke4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ke4 RCSB], [https://www.ebi.ac.uk/pdbsum/7ke4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ke4 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The SARS-CoV-2 spike (S) protein is the target of vaccine design efforts to end the COVID-19 pandemic. Despite a low mutation rate, isolates with the D614G substitution in the S protein appeared early during the pandemic, and are now the dominant form worldwide. Here, we analyze the D614G mutation in the context of a soluble S ectodomain construct. Cryo-EM structures, antigenicity and proteolysis experiments suggest altered conformational dynamics resulting in enhanced furin cleavage efficiency of the G614 variant. Furthermore, furin cleavage alters the conformational dynamics of the Receptor Binding Domains (RBD) in the G614 S ectodomain, demonstrating an allosteric effect on the RBD dynamics triggered by changes in the SD2 region, that harbors residue 614 and the furin cleavage site. Our results elucidate SARS-CoV-2 spike conformational dynamics and allostery, and have implications for vaccine design. | |||
D614G mutation alters SARS-CoV-2 spike conformational dynamics and protease cleavage susceptibility at the S1/S2 junction.,Gobeil S, Janowska K, McDowell S, Mansouri K, Parks R, Manne K, Stalls V, Kopp M, Henderson R, Edwards RJ, Haynes BF, Acharya P bioRxiv. 2020 Oct 12. doi: 10.1101/2020.10.11.335299. PMID:33052347<ref>PMID:33052347</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7ke4" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
==See Also== | |||
*[[Spike protein 3D structures|Spike protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Acharya P]] | |||
[[Category: Gobeil S]] | |||
Latest revision as of 09:28, 21 November 2024
SARS-CoV-2 D614G 3 RBD down Spike Protein Trimer without the P986-P987 stabilizing mutations (S-GSAS-D614G Sub-class)SARS-CoV-2 D614G 3 RBD down Spike Protein Trimer without the P986-P987 stabilizing mutations (S-GSAS-D614G Sub-class)
Structural highlights
Publication Abstract from PubMedThe SARS-CoV-2 spike (S) protein is the target of vaccine design efforts to end the COVID-19 pandemic. Despite a low mutation rate, isolates with the D614G substitution in the S protein appeared early during the pandemic, and are now the dominant form worldwide. Here, we analyze the D614G mutation in the context of a soluble S ectodomain construct. Cryo-EM structures, antigenicity and proteolysis experiments suggest altered conformational dynamics resulting in enhanced furin cleavage efficiency of the G614 variant. Furthermore, furin cleavage alters the conformational dynamics of the Receptor Binding Domains (RBD) in the G614 S ectodomain, demonstrating an allosteric effect on the RBD dynamics triggered by changes in the SD2 region, that harbors residue 614 and the furin cleavage site. Our results elucidate SARS-CoV-2 spike conformational dynamics and allostery, and have implications for vaccine design. D614G mutation alters SARS-CoV-2 spike conformational dynamics and protease cleavage susceptibility at the S1/S2 junction.,Gobeil S, Janowska K, McDowell S, Mansouri K, Parks R, Manne K, Stalls V, Kopp M, Henderson R, Edwards RJ, Haynes BF, Acharya P bioRxiv. 2020 Oct 12. doi: 10.1101/2020.10.11.335299. PMID:33052347[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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