8xqf

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Current revision (10:12, 22 January 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 8xqf is ON HOLD until 2026-04-05
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==Cryo-EM structure of human monomeric APJR-Gi complex with apelin-13.==
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<StructureSection load='8xqf' size='340' side='right'caption='[[8xqf]], [[Resolution|resolution]] 3.13&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8xqf]] is a 6 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=8XQF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8XQF FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.13&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8xqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xqf OCA], [https://pdbe.org/8xqf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xqf RCSB], [https://www.ebi.ac.uk/pdbsum/8xqf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xqf ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A096MZM0_PAPAN A0A096MZM0_PAPAN]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 8xqf" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Liu LE]]
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[[Category: Wu LJ]]
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[[Category: Xu F]]
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[[Category: Yue Y]]

Current revision

Cryo-EM structure of human monomeric APJR-Gi complex with apelin-13.

PDB ID 8xqf

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