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The entry | ==Structural impact on SARS-CoV-2 spike protein by D614G substitution== | ||
<StructureSection load='7krq' size='340' side='right'caption='[[7krq]], [[Resolution|resolution]] 3.44Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KRQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KRQ 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]] 3.44Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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=7krq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7krq OCA], [https://pdbe.org/7krq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7krq RCSB], [https://www.ebi.ac.uk/pdbsum/7krq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7krq ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Substitution for aspartic acid by glycine at position 614 in the spike (S) protein of severe acute respiratory syndrome coronavirus 2 appears to facilitate rapid viral spread. The G614 strain and its recent variants are now the dominant circulating forms. We report here cryo-EM structures of a full-length G614 S trimer, which adopts three distinct prefusion conformations differing primarily by the position of one receptor-binding domain. A loop disordered in the D614 S trimer wedges between domains within a protomer in the G614 spike. This added interaction appears to prevent premature dissociation of the G614 trimer, effectively increasing the number of functional spikes and enhancing infectivity, and to modulate structural rearrangements for membrane fusion. These findings extend our understanding of viral entry and suggest an improved immunogen for vaccine development. | |||
Structural impact on SARS-CoV-2 spike protein by D614G substitution.,Zhang J, Cai Y, Xiao T, Lu J, Peng H, Sterling SM, Walsh RM Jr, Rits-Volloch S, Zhu H, Woosley AN, Yang W, Sliz P, Chen B Science. 2021 Mar 16. pii: science.abf2303. doi: 10.1126/science.abf2303. PMID:33727252<ref>PMID:33727252</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7krq" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: Lu | ==See Also== | ||
[[Category: | *[[Spike protein 3D structures|Spike protein 3D structures]] | ||
[[Category: Sliz | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Cai YF]] | ||
[[Category: | [[Category: Chen B]] | ||
[[Category: | [[Category: Lu JM]] | ||
[[Category: | [[Category: Peng HQ]] | ||
[[Category: Sliz P]] | |||
[[Category: Sterling SM]] | |||
[[Category: Volloch SR]] | |||
[[Category: Walsh Jr RM]] | |||
[[Category: Woosley AN]] | |||
[[Category: Xiao TS]] | |||
[[Category: Yang W]] | |||
[[Category: Zhang J]] | |||
[[Category: Zhu HS]] | |||
Latest revision as of 09:29, 21 November 2024
Structural impact on SARS-CoV-2 spike protein by D614G substitutionStructural impact on SARS-CoV-2 spike protein by D614G substitution
Structural highlights
Publication Abstract from PubMedSubstitution for aspartic acid by glycine at position 614 in the spike (S) protein of severe acute respiratory syndrome coronavirus 2 appears to facilitate rapid viral spread. The G614 strain and its recent variants are now the dominant circulating forms. We report here cryo-EM structures of a full-length G614 S trimer, which adopts three distinct prefusion conformations differing primarily by the position of one receptor-binding domain. A loop disordered in the D614 S trimer wedges between domains within a protomer in the G614 spike. This added interaction appears to prevent premature dissociation of the G614 trimer, effectively increasing the number of functional spikes and enhancing infectivity, and to modulate structural rearrangements for membrane fusion. These findings extend our understanding of viral entry and suggest an improved immunogen for vaccine development. Structural impact on SARS-CoV-2 spike protein by D614G substitution.,Zhang J, Cai Y, Xiao T, Lu J, Peng H, Sterling SM, Walsh RM Jr, Rits-Volloch S, Zhu H, Woosley AN, Yang W, Sliz P, Chen B Science. 2021 Mar 16. pii: science.abf2303. doi: 10.1126/science.abf2303. PMID:33727252[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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