4l3n
From Proteopedia
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| - | {{STRUCTURE_4l3n| PDB=4l3n | SCENE= }} | ||
| - | ===Crystal structure of the receptor-binding domain from newly emerged Middle East respiratory syndrome coronavirus=== | ||
| - | == | + | ==Crystal structure of the receptor-binding domain from newly emerged Middle East respiratory syndrome coronavirus== |
| - | [[4l3n]] is a 2 chain structure with sequence from [ | + | <StructureSection load='4l3n' size='340' side='right'caption='[[4l3n]], [[Resolution|resolution]] 2.13Å' scene=''> |
| - | [[ | + | == Structural highlights == |
| - | [[ | + | <table><tr><td colspan='2'>[[4l3n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_betacoronavirus_2c_Jordan-N3/2012 Human betacoronavirus 2c Jordan-N3/2012]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L3N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L3N FirstGlance]. <br> |
| - | [[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.13Å</td></tr> |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=4l3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l3n OCA], [https://pdbe.org/4l3n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l3n RCSB], [https://www.ebi.ac.uk/pdbsum/4l3n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l3n ProSAT]</span></td></tr> |
| - | [[Category: | + | </table> |
| - | [[Category: | + | == Function == |
| - | [[Category: | + | [https://www.uniprot.org/uniprot/M4SVE7_MERS M4SVE7_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] |
| - | [[Category: | + | <div style="background-color:#fffaf0;"> |
| - | [[Category: | + | == Publication Abstract from PubMed == |
| - | [[Category: | + | The newly emerged Middle East respiratory syndrome coronavirus (MERS-CoV) has infected at least 77 people with a fatality rate of more than 50%. Alarmingly, the virus demonstrates a capability of human-to-human transmission, raising the possibility of global spread and endangering world health and economy. Here we have identified the receptor-binding domain (RBD) from the MERS-CoV spike protein and determined its crystal structure. This study also presents the structural comparison of MERS-CoV RBD with other coronavirus RBDs, successfully positioning MERS-CoV on the landscape of coronavirus evolution and providing insights into receptor binding by MERS-CoV. Furthermore, we found that MERS-CoV RBD functions as an effective entry inhibitor of MERS-CoV. The identified MERS-CoV RBD may also serve as a potential candidate for MERS-CoV subunit vaccines. Overall, this study enhances our understanding of the evolution of coronavirus RBDs, provides insights into receptor recognition by MERS-CoV, and may help control the transmission of MERS-CoV in humans. |
| + | |||
| + | Crystal structure of the receptor-binding domain from newly emerged Middle East respiratory syndrome coronavirus.,Chen Y, Rajashankar KR, Yang Y, Agnihothram SS, Liu C, Lin YL, Baric RS, Li F J Virol. 2013 Jul 31. PMID:23903833<ref>PMID:23903833</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4l3n" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human betacoronavirus 2c Jordan-N3/2012]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Agnihothram SS]] | ||
| + | [[Category: Baric RS]] | ||
| + | [[Category: Chen Y]] | ||
| + | [[Category: Li F]] | ||
| + | [[Category: Lin Y-L]] | ||
| + | [[Category: Liu C]] | ||
| + | [[Category: Rajashankar KR]] | ||
| + | [[Category: Yang Y]] | ||
Current revision
Crystal structure of the receptor-binding domain from newly emerged Middle East respiratory syndrome coronavirus
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