View source for 7ewr


==Cryo-EM structure of human GPR158 in complex with RGS7-Gbeta5 in a 2:2:2 ratio==
<StructureSection load='7ewr' size='340' side='right'caption='[[7ewr]], [[Resolution|resolution]] 4.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7ewr]] 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=7EWR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EWR 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]] 4.7&#8491;</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=7ewr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ewr OCA], [https://pdbe.org/7ewr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ewr RCSB], [https://www.ebi.ac.uk/pdbsum/7ewr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ewr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RGS7_HUMAN RGS7_HUMAN] Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Activity on G(o)-alpha is specifically enhanced by the RGS6/GNG5 dimer. May play a role in synaptic vesicle exocytosis. May play important role in the rapid regulation of neuronal excitability and the cellular responses to short-lived stimulations (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
GPR158, a class C orphan GPCR, functions in cognition, stress-induced mood control, and synaptic development. Among class C GPCRs, GPR158 is unique as it lacks a Venus flytrap-fold ligand-binding domain and terminates Galphai/o protein signaling through the RGS7-Gbeta5 heterodimer. Here, we report the cryo-EM structures of GPR158 alone and in complex with one or two RGS7-Gbeta5 heterodimers. GPR158 dimerizes through Per-Arnt-Sim-fold extracellular and transmembrane (TM) domains connected by an epidermal growth factor-like linker. The TM domain (TMD) reflects both inactive and active states of other class C GPCRs: a compact intracellular TMD, conformations of the two intracellular loops (ICLs) and the TMD interface formed by TM4/5. The ICL2, ICL3, TM3, and first helix of the cytoplasmic coiled-coil provide a platform for the DHEX domain of one RGS7 and the second helix recruits another RGS7. The unique features of the RGS7-binding site underlie the selectivity of GPR158 for RGS7.

Structure of the class C orphan GPCR GPR158 in complex with RGS7-Gbeta5.,Jeong E, Kim Y, Jeong J, Cho Y Nat Commun. 2021 Nov 23;12(1):6805. doi: 10.1038/s41467-021-27147-1. PMID:34815401<ref>PMID:34815401</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 7ewr" style="background-color:#fffaf0;"></div>

==See Also==
*[[Regulator of G-protein signaling 3D structures|Regulator of G-protein signaling 3D structures]]
*[[Transducin 3D structures|Transducin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Cho Y]]
[[Category: Jeong E]]
[[Category: Jeong J]]
[[Category: Kim Y]]