8c5r
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Omicron B.1.1.529 2 RBD up conformation== | |
| - | + | <StructureSection load='8c5r' size='340' side='right'caption='[[8c5r]], [[Resolution|resolution]] 3.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[8c5r]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Alphacoronavirus Alphacoronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8C5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8C5R FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.7Å</td></tr> | |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8c5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8c5r OCA], [https://pdbe.org/8c5r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8c5r RCSB], [https://www.ebi.ac.uk/pdbsum/8c5r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8c5r ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A6M4AIH4_SARS2 A0A6M4AIH4_SARS2] Spike protein S1: attaches the virion to the cell membrane by interacting with host receptor, initiating the infection.[HAMAP-Rule:MF_04099] Spike protein S2': Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.[HAMAP-Rule:MF_04099] Spike protein S2: 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] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Alphacoronavirus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Barfod LK]] | ||
| + | [[Category: Raghavan SSR]] | ||
| + | [[Category: Salanti A]] | ||
| + | [[Category: Walker MR]] | ||
| + | [[Category: Wang KT]] | ||
Revision as of 11:24, 24 January 2024
Omicron B.1.1.529 2 RBD up conformation
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