View source for 9rbq


==Semliki Forest virus trimer 1 in complex with ApoER2 LA5==
<StructureSection load='9rbq' size='340' side='right'caption='[[9rbq]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9rbq]] is a 13 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Semliki_Forest_virus Semliki Forest virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9RBQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9RBQ 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]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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=9rbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9rbq OCA], [https://pdbe.org/9rbq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9rbq RCSB], [https://www.ebi.ac.uk/pdbsum/9rbq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9rbq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GCAA_MOUSE GCAA_MOUSE] [https://www.uniprot.org/uniprot/E9PKG2_HUMAN E9PKG2_HUMAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The very low-density lipoprotein receptor (VLDLR) and apolipoprotein E receptor 2 (ApoER2) serve as entry receptors for the Semliki Forest virus (SFV). VLDLR interacts with the SFV E1 domain III (DIII) through multiple LDLR class A (LA) domains. However, the ApoER2-mediated SFV entry mechanism remains unclear. Here, we perform biochemical and cellular results and determine the cryogenic electron microscopy (cryo-EM) structures of SFV complexed with ApoER2 LA5 and full-length ApoER2, demonstrating that among the seven LA domains of ApoER2 isoform 1, only LA5 specifically binds to the SFV E1-DIII via a limited interface (353 A(2)) and facilitates cell attachment and entry. Site-directed mutagenesis confirms the significance of the residues at the SFV-ApoER2 interface. Significantly, a soluble LA5 decoy receptor neutralizes SFV infection and protects mice from lethal SFV challenge. These findings reveal a LA5-dependent receptor engagement mechanism for SFV entry via ApoER2, distinct from VLDLR.

Molecular basis of ApoER2-mediated Semliki Forest virus entry.,Du B, Song X, Zhao B, Shi Z, Liu Z, Wang S, Wei L, He X, Huiskonen JT, Yang D, Wang J Nat Commun. 2025 Dec 19. doi: 10.1038/s41467-025-67550-6. PMID:41419770<ref>PMID:41419770</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9rbq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Semliki Forest virus]]
[[Category: Du B]]
[[Category: Huiskonen JT]]
[[Category: Song X]]
[[Category: Wang J]]
[[Category: Yang D]]