9e96
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==WEEV CBA87 VLP in complex with human PCDH10-EC1== | |
| + | <StructureSection load='9e96' size='340' side='right'caption='[[9e96]], [[Resolution|resolution]] 4.05Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9e96]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Western_equine_encephalitis_virus Western equine encephalitis virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9E96 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9E96 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]] 4.05Å</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=9e96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9e96 OCA], [https://pdbe.org/9e96 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9e96 RCSB], [https://www.ebi.ac.uk/pdbsum/9e96 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9e96 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q1W679_WEEV Q1W679_WEEV] | ||
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 9e96" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Western equine encephalitis virus]] | ||
| + | [[Category: Diamond MS]] | ||
| + | [[Category: Fremont DH]] | ||
| + | [[Category: Raju S]] | ||
Current revision
WEEV CBA87 VLP in complex with human PCDH10-EC1
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