View source for 7wy0


==GPR110/G13 complex==
<StructureSection load='7wy0' size='340' side='right'caption='[[7wy0]], [[Resolution|resolution]] 2.83&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7wy0]] is a 5 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=7WY0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WY0 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]] 2.83&#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=7wy0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wy0 OCA], [https://pdbe.org/7wy0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wy0 RCSB], [https://www.ebi.ac.uk/pdbsum/7wy0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wy0 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Adhesion G protein-coupled receptors (aGPCRs) are keys of many physiological events and attractive targets for various diseases. aGPCRs are also known to be capable of self-activation via an autoproteolysis process that removes the inhibitory GAIN domain on the extracellular side of receptor and releases a stalk peptide to bind and activate the transmembrane side of receptor. However, the detailed mechanism of aGPCR activation remains elusive. Here, we report the cryo-electron microscopy structures of GPR110 (ADGRF1), a member of aGPCR, in complex with G(q), G(s), G(i), G(12) and G(13.) The structures reveal distinctive ligand engaging model and activation conformations of GPR110. The structures also unveil the rarely explored GPCR/G(12) and GPCR/G(13) engagements. A comparison of G(q), G(s), G(i), G(12) and G(13) engagements with GPR110 reveals details of G-protein engagement, including a dividing point at the far end of the alpha helix 5 (alphaH5) of Galpha subunit that separates G(q)/G(s) engagements from G(i)/G(12)/G(13) engagements. This is also where G(q)/G(s) bind the receptor through both hydrophobic and polar interaction, while G(i)/G(12)/G(13) engage receptor mainly through hydrophobic interaction. We further provide physiological evidence of GPR110 activation via stalk peptide. Taken together, our study fills the missing information of GPCR/G-protein engagement and provides a framework for understanding aGPCR activation and GPR110 signaling.

Structural basis of adhesion GPCR GPR110 activation by stalk peptide and G-proteins coupling.,Zhu X, Qian Y, Li X, Xu Z, Xia R, Wang N, Liang J, Yin H, Zhang A, Guo C, Wang G, He Y Nat Commun. 2022 Sep 20;13(1):5513. doi: 10.1038/s41467-022-33173-4. PMID:36127364<ref>PMID:36127364</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7wy0" style="background-color:#fffaf0;"></div>

==See Also==
*[[Transducin 3D structures|Transducin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: He Y]]
[[Category: Zhu X]]