8ufa
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Eastern equine encephalitis virus (PE-6) VLP (asymmetric unit)== | |
| + | <StructureSection load='8ufa' size='340' side='right'caption='[[8ufa]], [[Resolution|resolution]] 2.86Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8ufa]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Eastern_equine_encephalitis_virus Eastern equine encephalitis virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8UFA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8UFA 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]] 2.86Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=8ufa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ufa OCA], [https://pdbe.org/8ufa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ufa RCSB], [https://www.ebi.ac.uk/pdbsum/8ufa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ufa ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q88678_EEEV Q88678_EEEV] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The very-low-density lipoprotein receptor (VLDLR) comprises eight LDLR type A (LA) domains and supports entry of distantly related alphaviruses, including Eastern equine encephalitis virus (EEEV) and Semliki Forest virus (SFV). Here, by resolving multiple cryo-electron microscopy structures of EEEV-VLDLR complexes and performing mutagenesis and functional studies, we show that EEEV uses multiple sites (E1/E2 cleft and E2 A domain) to engage more than one LA domain simultaneously. However, no single LA domain is necessary or sufficient to support efficient EEEV infection. Whereas all EEEV strains show conservation of two VLDLR-binding sites, the EEEV PE-6 strain and a few other EEE complex members feature a single amino acid substitution that enables binding of LA domains to an additional site on the E2 B domain. These structural and functional analyses informed the design of a minimal VLDLR decoy receptor that neutralizes EEEV infection and protects mice from lethal challenge. | ||
| - | + | Structural and functional basis of VLDLR usage by Eastern equine encephalitis virus.,Adams LJ, Raju S, Ma H, Gilliland T Jr, Reed DS, Klimstra WB, Fremont DH, Diamond MS Cell. 2023 Dec 28:S0092-8674(23)01318-1. doi: 10.1016/j.cell.2023.11.031. PMID:38176410<ref>PMID:38176410</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8ufa" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Eastern equine encephalitis virus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Adams LJ]] | ||
| + | [[Category: Fremont DH]] | ||
Revision as of 10:10, 17 January 2024
Eastern equine encephalitis virus (PE-6) VLP (asymmetric unit)
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