7sxr
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='7sxr' size='340' side='right'caption='[[7sxr]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='7sxr' size='340' side='right'caption='[[7sxr]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SXR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SXR 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></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]] 3Å</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=7sxr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sxr OCA], [https://pdbe.org/7sxr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sxr RCSB], [https://www.ebi.ac.uk/pdbsum/7sxr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sxr 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=7sxr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sxr OCA], [https://pdbe.org/7sxr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sxr RCSB], [https://www.ebi.ac.uk/pdbsum/7sxr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sxr 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 18: | Line 17: | ||
</div> | </div> | ||
<div class="pdbe-citations 7sxr" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 7sxr" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Spike protein 3D structures|Spike protein 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 23: | Line 25: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Berezuk | + | [[Category: Berezuk AM]] |
| - | [[Category: Dimitrov | + | [[Category: Dimitrov DS]] |
| - | [[Category: Kim | + | [[Category: Kim A]] |
| - | [[Category: Li | + | [[Category: Li W]] |
| - | [[Category: Mannar | + | [[Category: Mannar D]] |
| - | [[Category: Saville | + | [[Category: Saville JW]] |
| - | [[Category: Srivastava | + | [[Category: Srivastava SS]] |
| - | [[Category: Subramaniam | + | [[Category: Subramaniam S]] |
| - | [[Category: Tuttle | + | [[Category: Tuttle KS]] |
| - | [[Category: Zhou | + | [[Category: Zhou S]] |
| - | [[Category: Zhu | + | [[Category: Zhu X]] |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Cryo-EM structure of the SARS-CoV-2 D614G mutant spike protein ectodomain
| |||||||||||
Categories: Large Structures | Berezuk AM | Dimitrov DS | Kim A | Li W | Mannar D | Saville JW | Srivastava SS | Subramaniam S | Tuttle KS | Zhou S | Zhu X
