7wz7: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7wz7]] 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=7WZ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WZ7 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7wz7]] 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=7WZ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WZ7 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=7wz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wz7 OCA], [https://pdbe.org/7wz7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wz7 RCSB], [https://www.ebi.ac.uk/pdbsum/7wz7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wz7 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]] 2.83Å</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=7wz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wz7 OCA], [https://pdbe.org/7wz7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wz7 RCSB], [https://www.ebi.ac.uk/pdbsum/7wz7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wz7 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/GBB1_HUMAN GBB1_HUMAN] Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.<ref>PMID:18611381</ref> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7wz7" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Transducin 3D structures|Transducin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Latest revision as of 17:11, 6 November 2024
GPR110/G12 complexGPR110/G12 complex
Structural highlights
FunctionGBB1_HUMAN Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.[1] Publication Abstract from PubMedAdhesion 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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