View source for 8xqi


==Cryo-EM structure of human dimeric Apelin receptor.==
<StructureSection load='8xqi' size='340' side='right'caption='[[8xqi]], [[Resolution|resolution]] 3.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8xqi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8XQI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8XQI 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]] 3.25&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</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=8xqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xqi OCA], [https://pdbe.org/8xqi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xqi RCSB], [https://www.ebi.ac.uk/pdbsum/8xqi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xqi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/APJ_HUMAN APJ_HUMAN] Receptor for apelin coupled to G proteins that inhibit adenylate cyclase activity. Alternative coreceptor with CD4 for HIV-1 infection; may be involved in the development of AIDS dementia.[https://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX] Electron-transport protein of unknown function.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The apelin receptor (APJR) emerges as a promising drug target for cardiovascular health and muscle regeneration. While prior research unveiled the structural versatility of APJR in coupling to Gi proteins as a monomer or dimer, the dynamic regulation within the APJR dimer during activation remains poorly understood. In this study, we present the structures of the APJR dimer and monomer complexed with its endogenous ligand apelin-13. In the dimeric structure, apelin-13 binds exclusively to one protomer that is coupled with Gi proteins, revealing a distinct ligand-binding behavior within APJR homodimers. Furthermore, binding of an antagonistic antibody induces a more compact dimerization by engaging both protomers. Notably, structural analyses of the APJR dimer complexed with an agonistic antibody, with or without Gi proteins, suggest that G protein coupling may promote the dissociation of the APJR dimer during activation. These findings underscore the intricate interplay between ligands, dimerization, and G protein coupling in regulating APJR signaling pathways.

Structural insights into the regulation of monomeric and dimeric apelin receptor.,Yue Y, Liu L, Wu L, Xu C, Na M, Liu S, Liu Y, Li F, Liu J, Shi S, Lei H, Zhao M, Yang T, Ji W, Wang A, Hanson MA, Stevens RC, Liu J, Xu F Nat Commun. 2025 Jan 2;16(1):310. doi: 10.1038/s41467-024-55555-6. PMID:39747115<ref>PMID:39747115</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8xqi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Liu LE]]
[[Category: Wu LJ]]
[[Category: Xu F]]
[[Category: Yue Y]]