View source for 7sxw


==Cryo-EM structure of the SARS-CoV-2 D614G,N501Y,E484K,K417T mutant spike protein ectodomain==
<StructureSection load='7sxw' size='340' side='right'caption='[[7sxw]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SXW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SXW 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]] 2.85&#8491;</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=7sxw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sxw OCA], [https://pdbe.org/7sxw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sxw RCSB], [https://www.ebi.ac.uk/pdbsum/7sxw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sxw ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The recently emerged severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) Beta (B.1.351) and Gamma (P.1) variants of concern (VoCs) include a key mutation (N501Y) found in the Alpha (B.1.1.7) variant that enhances affinity of the spike protein for its receptor, angiotensin-converting enzyme 2 (ACE2). Additional mutations are found in these variants at residues 417 and 484 that appear to promote antibody evasion. In contrast, the Epsilon variants (B.1.427/429) lack the N501Y mutation yet exhibit antibody evasion. We have engineered spike proteins to express these receptor binding domain (RBD) VoC mutations either in isolation or in different combinations and analyze the effects using biochemical assays and cryoelectron microscopy (cryo-EM) structural analyses. Overall, our findings suggest that the emergence of new SARS-CoV-2 variant spikes can be rationalized as the result of mutations that confer increased ACE2 affinity, increased antibody evasion, or both, providing a framework to dissect the molecular factors that drive VoC evolution.

Structural analysis of receptor binding domain mutations in SARS-CoV-2 variants of concern that modulate ACE2 and antibody binding.,Mannar D, Saville JW, Zhu X, Srivastava SS, Berezuk AM, Zhou S, Tuttle KS, Kim A, Li W, Dimitrov DS, Subramaniam S Cell Rep. 2021 Dec 21;37(12):110156. doi: 10.1016/j.celrep.2021.110156. Epub 2021, Dec 4. PMID:34914928<ref>PMID:34914928</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7sxw" style="background-color:#fffaf0;"></div>

==See Also==
*[[Spike protein 3D structures|Spike protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Berezuk AM]]
[[Category: Dimitrov DS]]
[[Category: Kim A]]
[[Category: Li W]]
[[Category: Mannar D]]
[[Category: Saville JW]]
[[Category: Srivastava SS]]
[[Category: Subramaniam S]]
[[Category: Tuttle KS]]
[[Category: Zhou S]]
[[Category: Zhu X]]