8ufc: Difference between revisions
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The entry | ==Eastern equine encephalitis virus (PE-6) VLP in complex with VLDLR LA(1-2) (asymmetric unit)== | ||
<StructureSection load='8ufc' size='340' side='right'caption='[[8ufc]], [[Resolution|resolution]] 3.09Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8ufc]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Eastern_equine_encephalitis_virus Eastern equine encephalitis virus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8UFC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8UFC 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]] 3.09Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=8ufc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ufc OCA], [https://pdbe.org/8ufc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ufc RCSB], [https://www.ebi.ac.uk/pdbsum/8ufc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ufc 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. 2024 Jan 18;187(2):360-374.e19. doi: 10.1016/j.cell.2023.11.031. Epub 2024 , Jan 3. 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 8ufc" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Eastern equine encephalitis virus]] | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Adams LJ]] | |||
[[Category: Fremont DH]] | |||
Latest revision as of 15:12, 30 October 2024
Eastern equine encephalitis virus (PE-6) VLP in complex with VLDLR LA(1-2) (asymmetric unit)Eastern equine encephalitis virus (PE-6) VLP in complex with VLDLR LA(1-2) (asymmetric unit)
Structural highlights
FunctionPublication Abstract from PubMedThe 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. 2024 Jan 18;187(2):360-374.e19. doi: 10.1016/j.cell.2023.11.031. Epub 2024 , Jan 3. PMID:38176410[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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