7n1h
From Proteopedia
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| - | ==== | + | ==CryoEM structure of Venezuelan equine encephalitis virus VLP in complex with the LDLRAD3 receptor== |
| - | < | + | <SX load='7n1h' size='340' side='right' viewer='molstar' caption='[[7n1h]], [[Resolution|resolution]] 4.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7n1h]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Venezuelan_equine_encephalitis_virus Venezuelan equine encephalitis virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7N1H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7N1H FirstGlance]. <br> |
| - | </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=7n1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7n1h OCA], [https://pdbe.org/7n1h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7n1h RCSB], [https://www.ebi.ac.uk/pdbsum/7n1h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7n1h ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.3Å</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=7n1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7n1h OCA], [https://pdbe.org/7n1h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7n1h RCSB], [https://www.ebi.ac.uk/pdbsum/7n1h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7n1h ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/LRAD3_MOUSE LRAD3_MOUSE] May influence APP processing, resulting in a decrease in sAPP-alpha production and increased amyloidogenic P3 peptide production (PubMed:21795536). May regulate ITCH and NEDD4 E3 ligase activity and degradation (By similarity).[UniProtKB:Q86YD5]<ref>PMID:21795536</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | LDLRAD3 is a recently defined attachment and entry receptor for Venezuelan equine encephalitis virus (VEEV)(1), a New World alphavirus that causes severe neurological disease in humans. Here we present near-atomic-resolution cryo-electron microscopy reconstructions of VEEV virus-like particles alone and in a complex with the ectodomains of LDLRAD3. Domain 1 of LDLRAD3 is a low-density lipoprotein receptor type-A module that binds to VEEV by wedging into a cleft created by two adjacent E2-E1 heterodimers in one trimeric spike, and engages domains A and B of E2 and the fusion loop in E1. Atomic modelling of this interface is supported by mutagenesis and anti-VEEV antibody binding competition assays. Notably, VEEV engages LDLRAD3 in a manner that is similar to the way that arthritogenic alphaviruses bind to the structurally unrelated MXRA8 receptor, but with a much smaller interface. These studies further elucidate the structural basis of alphavirus-receptor interactions, which could inform the development of therapies to mitigate infection and disease against multiple members of this family. | ||
| + | |||
| + | Structure of Venezuelan equine encephalitis virus in complex with the LDLRAD3 receptor.,Basore K, Ma H, Kafai NM, Mackin S, Kim AS, Nelson CA, Diamond MS, Fremont DH Nature. 2021 Oct;598(7882):672-676. doi: 10.1038/s41586-021-03963-9. Epub 2021 , Oct 13. PMID:34646020<ref>PMID:34646020</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7n1h" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
| - | </ | + | </SX> |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Mus musculus]] |
| + | [[Category: Venezuelan equine encephalitis virus]] | ||
| + | [[Category: Basore K]] | ||
| + | [[Category: Fremont DH]] | ||
| + | [[Category: Nelson CA]] | ||
Current revision
CryoEM structure of Venezuelan equine encephalitis virus VLP in complex with the LDLRAD3 receptor
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