8ufc: Difference between revisions

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-'''Unreleased structure'''
-The entry 8ufc is ON HOLD  until Paper Publication
+==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]] 3.09&Aring;' 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]] 3.09&#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>, <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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</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]]