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9uea
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Prefusion structure of GX2012 spike glycoprotein== | |
| - | + | <StructureSection load='9uea' size='340' side='right'caption='[[9uea]], [[Resolution|resolution]] 2.94Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[9uea]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/BtTp-BetaCoV/GX2012 BtTp-BetaCoV/GX2012]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9UEA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9UEA 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]] 2.94Å</td></tr> | |
| - | [[Category: | + | <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=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=9uea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9uea OCA], [https://pdbe.org/9uea PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9uea RCSB], [https://www.ebi.ac.uk/pdbsum/9uea PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9uea ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A0U1WJZ6_BCHK4 A0A0U1WJZ6_BCHK4] 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: BtTp-BetaCoV/GX2012]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Lin Z]] | ||
| + | [[Category: Wang X]] | ||
Current revision
Prefusion structure of GX2012 spike glycoprotein
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