7wy8
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7wy8]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Lama_glama Lama glama] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WY8 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7wy8]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Lama_glama Lama glama] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WY8 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=7wy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wy8 OCA], [https://pdbe.org/7wy8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wy8 RCSB], [https://www.ebi.ac.uk/pdbsum/7wy8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wy8 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=7wy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wy8 OCA], [https://pdbe.org/7wy8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wy8 RCSB], [https://www.ebi.ac.uk/pdbsum/7wy8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wy8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/AGRL3_MOUSE AGRL3_MOUSE] Plays a role in cell-cell adhesion and neuron guidance via its interactions with FLRT2 and FLRT3 that are expressed at the surface of adjacent cells (PubMed:22405201, PubMed:25728924, PubMed:26235031). Plays a role in the development of glutamatergic synapses in the cortex (PubMed:22405201, PubMed:24739570). Important in determining the connectivity rates between the principal neurons in the cortex (PubMed:24739570).<ref>PMID:22405201</ref> <ref>PMID:24739570</ref> <ref>PMID:25728924</ref> <ref>PMID:26235031</ref> | [https://www.uniprot.org/uniprot/AGRL3_MOUSE AGRL3_MOUSE] Plays a role in cell-cell adhesion and neuron guidance via its interactions with FLRT2 and FLRT3 that are expressed at the surface of adjacent cells (PubMed:22405201, PubMed:25728924, PubMed:26235031). Plays a role in the development of glutamatergic synapses in the cortex (PubMed:22405201, PubMed:24739570). Important in determining the connectivity rates between the principal neurons in the cortex (PubMed:24739570).<ref>PMID:22405201</ref> <ref>PMID:24739570</ref> <ref>PMID:25728924</ref> <ref>PMID:26235031</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Adhesion G-protein-coupled receptors (aGPCRs) play key roles in a diversity of physiologies. A hallmark of aGPCR activation is the removal of the inhibitory GAIN domain and the dipping of the cleaved stalk peptide into the ligand-binding pocket of receptors; however, the detailed mechanism remains obscure. Here, we present cryoelectron microscopy (cryo-EM) structures of ADGRL3 in complex with G(q), G(s), G(i), and G(12). The structures reveal unique ligand-engaging mode, distinctive activation conformation, and key mechanisms of aGPCR activation. The structures also reveal the uncharted structural information of GPCR/G(12) coupling. A comparison of G(q), G(s), G(i), and G(12) engagements with ADGRL3 reveals the key determinant of G-protein coupling on the far end of alphaH5 of Galpha. A detailed analysis of the engagements allows us to design mutations that specifically enhance one pathway over others. Taken together, our study lays the groundwork for understanding aGPCR activation and G-protein-coupling selectivity. | ||
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| + | Structural insights into adhesion GPCR ADGRL3 activation and G(q), G(s), G(i), and G(12) coupling.,Qian Y, Ma Z, Liu C, Li X, Zhu X, Wang N, Xu Z, Xia R, Liang J, Duan Y, Yin H, Xiong Y, Zhang A, Guo C, Chen Z, Huang Z, He Y Mol Cell. 2022 Nov 17;82(22):4340-4352.e6. doi: 10.1016/j.molcel.2022.10.009. , Epub 2022 Oct 28. PMID:36309016<ref>PMID:36309016</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7wy8" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Latrophilin|Latrophilin]] | ||
| + | *[[Transducin 3D structures|Transducin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
ADGRL3/Gs complex
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