View source for 9eau


==RRV DKTA VLP in complex with VLDLR-LBD-Fc==
<StructureSection load='9eau' size='340' side='right'caption='[[9eau]], [[Resolution|resolution]] 3.06&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9eau]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Ross_river_virus_(STRAIN_T48) Ross river virus (STRAIN T48)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9EAU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9EAU 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]] 3.06&#8491;</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></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=9eau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9eau OCA], [https://pdbe.org/9eau PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9eau RCSB], [https://www.ebi.ac.uk/pdbsum/9eau PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9eau ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C9DZM3_9VIRU C9DZM3_9VIRU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structural basis for shifts in receptor usage remains poorly understood despite the implications for virus adaptation and emergence. Western equine encephalitis virus (WEEV) strains exhibit different patterns of engagement for two of their entry receptors: very-low-density lipoprotein receptor (VLDLR) and protocadherin 10 (PCDH10). Using structural and functional studies, we show that while all WEEV strains have a lipoprotein class A (LA) domain binding site near the E1 fusion loop, VLDLR engagement requires a second binding site in E2 that can vary with single nucleotide substitutions. We also resolve a structure of PCDH10 bound to WEEV, which reveals interactions near the E1 fusion loop with residues that also mediate LA domain binding. Evolutionary analysis enabled the generation of a PCDH10 decoy that protects in vivo against all WEEV strains tested. Our experiments demonstrate how viruses can engage multiple receptors using shared determinants, which likely impacts cellular tropism and virulence.

Structural basis for plasticity in receptor engagement by an encephalitic alphavirus.,Raju S, Palakurty S, Sariol A, Wagoner N, Adams LJ, Hui S, Klimstra WB, Fremont DH, Diamond MS Cell. 2025 Apr 4:S0092-8674(25)00272-7. doi: 10.1016/j.cell.2025.02.036. PMID:40187344<ref>PMID:40187344</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9eau" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Diamond MS]]
[[Category: Fremont DH]]
[[Category: Raju S]]