7a57
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7a57]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/La_Crosse_virus_L78 La Crosse virus L78]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7A57 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7A57 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7a57]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/La_Crosse_virus_L78 La Crosse virus L78]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7A57 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7A57 FirstGlance]. <br> | ||
| - | </td></tr><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.155Å</td></tr> |
| + | <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=7a57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a57 OCA], [https://pdbe.org/7a57 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7a57 RCSB], [https://www.ebi.ac.uk/pdbsum/7a57 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7a57 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=7a57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a57 OCA], [https://pdbe.org/7a57 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7a57 RCSB], [https://www.ebi.ac.uk/pdbsum/7a57 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7a57 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/GP_BUNL8 GP_BUNL8] Glycoprotein C and glycoprotein N interact with each other and are present at the surface of the virion. They are able to attach the virion to a cell receptor and to promote fusion of membranes after endocytosis of the virion (By similarity). | [https://www.uniprot.org/uniprot/GP_BUNL8 GP_BUNL8] Glycoprotein C and glycoprotein N interact with each other and are present at the surface of the virion. They are able to attach the virion to a cell receptor and to promote fusion of membranes after endocytosis of the virion (By similarity). | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | La Crosse virus, responsible for pediatric encephalitis in the United States, and Schmallenberg virus, a highly teratogenic veterinary virus in Europe, belong to the large Orthobunyavirus genus of zoonotic arthropod-borne pathogens distributed worldwide. Viruses in this under-studied genus cause CNS infections or fever with debilitating arthralgia/myalgia syndromes, with no effective treatment. The main surface antigen, glycoprotein Gc ( approximately 1,000 residues), has a variable N-terminal half (Gc(S)) targeted by the patients' antibody response and a conserved C-terminal moiety (Gc(F)) responsible for membrane fusion during cell entry. Here, we report the X-ray structure of post-fusion La Crosse and Schmallenberg virus Gc(F), revealing the molecular determinants for hairpin formation and trimerization required to drive membrane fusion. We further experimentally confirm the role of residues in the fusion loops and in a vestigial endoplasmic reticulum (ER) translocation sequence at the Gc(S)-Gc(F) junction. The resulting knowledge provides essential molecular underpinnings for future development of potential therapeutic treatments and vaccines. | ||
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| - | Structure, function, and evolution of the Orthobunyavirus membrane fusion glycoprotein.,Hellert J, Aebischer A, Haouz A, Guardado-Calvo P, Reiche S, Beer M, Rey FA Cell Rep. 2023 Feb 22;42(3):112142. doi: 10.1016/j.celrep.2023.112142. PMID:36827185<ref>PMID:36827185</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 7a57" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 07:51, 7 February 2024
La Crosse Virus Envelope Glycoprotein Gc W1066H Mutant Fusion Domains in Postfusion Conformation
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