7qdh

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Current revision (13:55, 6 November 2024) (edit) (undo)
 
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<StructureSection load='7qdh' size='340' side='right'caption='[[7qdh]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
<StructureSection load='7qdh' size='340' side='right'caption='[[7qdh]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7qdh]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QDH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QDH FirstGlance]. <br>
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QDH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QDH FirstGlance]. <br>
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</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>
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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]] 4.2&#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=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=7qdh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qdh OCA], [https://pdbe.org/7qdh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qdh RCSB], [https://www.ebi.ac.uk/pdbsum/7qdh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qdh 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=7qdh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qdh OCA], [https://pdbe.org/7qdh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qdh RCSB], [https://www.ebi.ac.uk/pdbsum/7qdh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qdh ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
 
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[[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]
 
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The S:A222V point mutation, within the G clade, was characteristic of the 20E (EU1) SARS-CoV-2 variant identified in Spain in early summer 2020. This mutation has since reappeared in the Delta subvariant AY.4.2, raising questions about its specific effect on viral infection. We report combined serological, functional, structural and computational studies characterizing the impact of this mutation. Our results reveal that S:A222V promotes an increased RBD opening and slightly increases ACE2 binding as compared to the parent S:D614G clade. Finally, S:A222V does not reduce sera neutralization capacity, suggesting it does not affect vaccine effectiveness.
 
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The structural role of SARS-CoV-2 genetic background in the emergence and success of spike mutations: The case of the spike A222V mutation.,Ginex T, Marco-Marin C, Wieczor M, Mata CP, Krieger J, Ruiz-Rodriguez P, Lopez-Redondo ML, Frances-Gomez C, Melero R, Sanchez-Sorzano CO, Martinez M, Gougeard N, Forcada-Nadal A, Zamora-Caballero S, Gozalbo-Rovira R, Sanz-Frasquet C, Arranz R, Bravo J, Rubio V, Marina A, Geller R, Comas I, Gil C, Coscolla M, Orozco M, Llacer JL, Carazo JM PLoS Pathog. 2022 Jul 11;18(7):e1010631. doi: 10.1371/journal.ppat.1010631., eCollection 2022 Jul. PMID:35816514<ref>PMID:35816514</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 7qdh" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bravo, J]]
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[[Category: Bravo J]]
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[[Category: Carazo, J M]]
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[[Category: Carazo JM]]
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[[Category: Comas, I]]
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[[Category: Comas I]]
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[[Category: Coscolla, M]]
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[[Category: Coscolla M]]
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[[Category: Forcada-Nadal, A]]
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[[Category: Forcada-Nadal A]]
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[[Category: Frances-Gomez, C]]
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[[Category: Frances-Gomez C]]
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[[Category: Geller, R]]
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[[Category: Geller R]]
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[[Category: Gil, C]]
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[[Category: Gil C]]
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[[Category: Ginex, T]]
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[[Category: Ginex T]]
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[[Category: Gougeard, N]]
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[[Category: Gougeard N]]
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[[Category: Gozalbo-Rovira, R]]
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[[Category: Gozalbo-Rovira R]]
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[[Category: Krieger, J]]
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[[Category: Krieger J]]
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[[Category: LLacer, J L]]
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[[Category: LLacer JL]]
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[[Category: Lopez-Redondo, M L]]
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[[Category: Lopez-Redondo ML]]
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[[Category: Marco-Marin, C]]
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[[Category: Marco-Marin C]]
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[[Category: Marina, A]]
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[[Category: Marina A]]
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[[Category: Martinez, M]]
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[[Category: Martinez M]]
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[[Category: Mata, C P]]
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[[Category: Mata CP]]
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[[Category: Melero, R]]
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[[Category: Melero R]]
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[[Category: Orozco, M]]
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[[Category: Orozco M]]
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[[Category: Rubio, V]]
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[[Category: Rubio V]]
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[[Category: Ruiz-Rodriguez, P]]
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[[Category: Ruiz-Rodriguez P]]
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[[Category: Sanchez-Sorzano, C O]]
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[[Category: Sanchez-Sorzano CO]]
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[[Category: Sanz-Frasquet, C]]
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[[Category: Sanz-Frasquet C]]
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[[Category: Wieczor, M]]
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[[Category: Wieczor M]]
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[[Category: Zamora-Caballero, S]]
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[[Category: Zamora-Caballero S]]
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[[Category: S protein]]
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[[Category: S:d614g mutant]]
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[[Category: Sars-cov-2]]
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[[Category: Viral protein]]
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Current revision

SARS-CoV-2 S protein S:D614G mutant 1-up

PDB ID 7qdh

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