7thk
From Proteopedia
(Difference between revisions)
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==Cryo-EM structure of prefusion SARS-CoV-2 spike omicron B.1.1.529 variant== | ==Cryo-EM structure of prefusion SARS-CoV-2 spike omicron B.1.1.529 variant== | ||
| - | <StructureSection load='7thk' size='340' side='right'caption='[[7thk]]' scene=''> | + | <StructureSection load='7thk' size='340' side='right'caption='[[7thk]], [[Resolution|resolution]] 3.11Å' 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=7THK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7THK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7thk]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7THK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7THK FirstGlance]. <br> |
| - | </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=7thk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7thk OCA], [https://pdbe.org/7thk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7thk RCSB], [https://www.ebi.ac.uk/pdbsum/7thk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7thk ProSAT]</span></td></tr> | + | </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=7thk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7thk OCA], [https://pdbe.org/7thk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7thk RCSB], [https://www.ebi.ac.uk/pdbsum/7thk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7thk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/SPIKE_SARS2 SPIKE_SARS2]] attaches the virion to the cell membrane by interacting with host receptor, initiating the infection (By similarity). Binding to human ACE2 receptor and internalization of the virus into the endosomes of the host cell induces conformational changes in the Spike glycoprotein (PubMed:32142651, PubMed:32075877, PubMed:32155444). Uses also human TMPRSS2 for priming in human lung cells which is an essential step for viral entry (PubMed:32142651). Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes.[HAMAP-Rule:MF_04099]<ref>PMID:32075877</ref> <ref>PMID:32142651</ref> <ref>PMID:32155444</ref> mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes.[HAMAP-Rule:MF_04099] Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.[HAMAP-Rule:MF_04099] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The recently reported B.1.1.529 Omicron variant of severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) includes 34 mutations in the spike protein relative to the Wuhan strain, including 15 mutations in the receptor-binding domain (RBD). Functional studies have shown Omicron to substantially escape the activity of many SARS-CoV-2-neutralizing antibodies. Here, we report a 3.1 A-resolution cryoelectron microscopy (cryo-EM) structure of the Omicron spike protein ectodomain. The structure depicts a spike that is exclusively in the 1-RBD-up conformation with high mobility of RBD. Many mutations cause steric clashes and/or altered interactions at antibody-binding surfaces, whereas others mediate changes of the spike structure in local regions to interfere with antibody recognition. Overall, the structure of the Omicron spike reveals how mutations alter its conformation and explains its extraordinary ability to evade neutralizing antibodies. | ||
| + | |||
| + | Cryo-EM structure of the SARS-CoV-2 Omicron spike.,Cerutti G, Guo Y, Liu L, Liu L, Zhang Z, Luo Y, Huang Y, Wang HH, Ho DD, Sheng Z, Shapiro L Cell Rep. 2022 Feb 7:110428. doi: 10.1016/j.celrep.2022.110428. PMID:35172173<ref>PMID:35172173</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7thk" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Cerutti G]] | + | [[Category: Cerutti, G]] |
| - | [[Category: Shapiro L]] | + | [[Category: Shapiro, L]] |
| + | [[Category: Covid-19]] | ||
| + | [[Category: Fusion protein]] | ||
| + | [[Category: Ntd]] | ||
| + | [[Category: Rbd]] | ||
| + | [[Category: Spike glycoprotein]] | ||
| + | [[Category: Viral protein]] | ||
Revision as of 07:24, 16 March 2022
Cryo-EM structure of prefusion SARS-CoV-2 spike omicron B.1.1.529 variant
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