7ymw
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of MERS-CoV spike protein, One RBD-up conformation 4== | |
| - | + | <StructureSection load='7ymw' size='340' side='right'caption='[[7ymw]], [[Resolution|resolution]] 6.05Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[7ymw]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_betacoronavirus_2c_EMC/2012 Human betacoronavirus 2c EMC/2012]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YMW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YMW 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]] 6.05Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</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=7ymw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ymw OCA], [https://pdbe.org/7ymw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ymw RCSB], [https://www.ebi.ac.uk/pdbsum/7ymw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ymw ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/K0BRG7_MERS K0BRG7_MERS] 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: Human betacoronavirus 2c EMC/2012]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chang NE]] | ||
| + | [[Category: Draczkowski P]] | ||
| + | [[Category: Hsu STD]] | ||
| + | [[Category: Weng ZW]] | ||
| + | [[Category: Yang TJ]] | ||
Revision as of 05:21, 9 August 2023
Cryo-EM structure of MERS-CoV spike protein, One RBD-up conformation 4
| |||||||||||
