7n1t
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants== | |
| + | <StructureSection load='7n1t' size='340' side='right'caption='[[7n1t]], [[Resolution|resolution]] 3.44Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7n1t]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/2019-ncov 2019-ncov]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7N1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7N1T FirstGlance]. <br> | ||
| + | </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>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">S, 2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2697049 2019-nCoV])</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=7n1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7n1t OCA], [https://pdbe.org/7n1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7n1t RCSB], [https://www.ebi.ac.uk/pdbsum/7n1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7n1t ProSAT]</span></td></tr> | ||
| + | </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 == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7n1t" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: 2019-ncov]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Cai, Y F]] | ||
| + | [[Category: Chen, B]] | ||
| + | [[Category: Jr, R M.Walsh]] | ||
| + | [[Category: Peng, H Q]] | ||
[[Category: Rawson, S]] | [[Category: Rawson, S]] | ||
| - | + | [[Category: Sterling, S M]] | |
| - | [[Category: Sterling, S | + | [[Category: Volloch, S R]] |
| - | [[Category: | + | [[Category: Xiao, T S]] |
| - | [[Category: Xiao, T | + | |
[[Category: Zhang, J]] | [[Category: Zhang, J]] | ||
| - | [[Category: | + | [[Category: Viral protein]] |
| - | + | ||
| - | + | ||
Current revision
Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants
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Categories: 2019-ncov | Large Structures | Cai, Y F | Chen, B | Jr, R M.Walsh | Peng, H Q | Rawson, S | Sterling, S M | Volloch, S R | Xiao, T S | Zhang, J | Viral protein
