7n1v

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==Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants==
==Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants==
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<StructureSection load='7n1v' size='340' side='right'caption='[[7n1v]]' scene=''>
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<StructureSection load='7n1v' size='340' side='right'caption='[[7n1v]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7N1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7N1V FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7N1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7N1V FirstGlance]. <br>
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</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=7n1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7n1v OCA], [https://pdbe.org/7n1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7n1v RCSB], [https://www.ebi.ac.uk/pdbsum/7n1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7n1v ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7n1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7n1v OCA], [https://pdbe.org/7n1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7n1v RCSB], [https://www.ebi.ac.uk/pdbsum/7n1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7n1v ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Several fast-spreading variants of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have become the dominant circulating strains in the COVID-19 pandemic. We report here cryo-EM structures of the full-length spike (S) trimers of the B.1.1.7 and B.1.351 variants, as well as their biochemical and antigenic properties. Amino acid substitutions in the B.1.1.7 protein increase the accessibility of its receptor binding domain and also the binding affinity for receptor angiotensin-converting enzyme 2 (ACE2). The enhanced receptor engagement may account for the increased transmissibility. The B.1.351 variant has evolved to reshape antigenic surfaces of the major neutralizing sites on the S protein, making it resistant to some potent neutralizing antibodies. These findings provide structural details on how SARS-CoV-2 has evolved to enhance viral fitness and immune evasion.
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Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants.,Cai Y, Zhang J, Xiao T, Lavine CL, Rawson S, Peng H, Zhu H, Anand K, Tong P, Gautam A, Lu S, Sterling SM, Walsh RM Jr, Rits-Volloch S, Lu J, Wesemann DR, Yang W, Seaman MS, Chen B Science. 2021 Jun 24. pii: science.abi9745. doi: 10.1126/science.abi9745. PMID:34168070<ref>PMID:34168070</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7n1v" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants

PDB ID 7n1v

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