7sbr: Difference between revisions

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<StructureSection load='7sbr' size='340' side='right'caption='[[7sbr]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
<StructureSection load='7sbr' size='340' side='right'caption='[[7sbr]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7sbr]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SBR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SBR FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SBR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SBR 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>
</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>
<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=7sbr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sbr OCA], [https://pdbe.org/7sbr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sbr RCSB], [https://www.ebi.ac.uk/pdbsum/7sbr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sbr ProSAT]</span></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=7sbr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sbr OCA], [https://pdbe.org/7sbr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sbr RCSB], [https://www.ebi.ac.uk/pdbsum/7sbr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sbr 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 ==
[Figure: see text].


Membrane fusion and immune evasion by the spike protein of SARS-CoV-2 Delta variant.,Zhang J, Xiao T, Cai Y, Lavine CL, Peng H, Zhu H, Anand K, Tong P, Gautam A, Mayer ML, Walsh RM, Jr, Rits-Volloch S, Wesemann DR, Yang W, Seaman MS, Lu J, Chen B Science. 2021 Oct 26:eabl9463. doi: 10.1126/science.abl9463. PMID:34698504<ref>PMID:34698504</ref>
==See Also==
 
*[[Spike protein 3D structures|Spike protein 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7sbr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cai, Y F]]
[[Category: Cai YF]]
[[Category: Chen, B]]
[[Category: Chen B]]
[[Category: Peng, H Q]]
[[Category: Peng HQ]]
[[Category: Volloch, S R]]
[[Category: Volloch SR]]
[[Category: Xiao, T S]]
[[Category: Xiao TS]]
[[Category: Zhang, J]]
[[Category: Zhang J]]
[[Category: Viral protein]]

Latest revision as of 14:29, 23 October 2024

One RBD-up 2 of pre-fusion SARS-CoV-2 Kappa variant spike proteinOne RBD-up 2 of pre-fusion SARS-CoV-2 Kappa variant spike protein

Structural highlights

Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.5Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

See Also

7sbr, resolution 3.50Å

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