8id3

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Current revision (09:43, 17 October 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[8id3]] 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=8ID3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ID3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[8id3]] 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=8ID3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ID3 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7NR:9-Hydroxyoctadecanoic+acid'>7NR</scene></td></tr>
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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]] 3.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7NR:(9~{S})-9-oxidanyloctadecanoic+acid'>7NR</scene></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=8id3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8id3 OCA], [https://pdbe.org/8id3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8id3 RCSB], [https://www.ebi.ac.uk/pdbsum/8id3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8id3 ProSAT]</span></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=8id3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8id3 OCA], [https://pdbe.org/8id3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8id3 RCSB], [https://www.ebi.ac.uk/pdbsum/8id3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8id3 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
 
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[https://www.uniprot.org/uniprot/GBG2_HUMAN GBG2_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 (By similarity).
 
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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Individual free fatty acids (FAs) play important roles in metabolic homeostasis, many via engagement with more than 40 GPCRs. Searching for receptors to sense beneficial omega-3 FAs of fish oil enabled the identification of GPR120, involving with a spectrum of metabolic diseases. Here, we report six cryo-EM structures of GPR120 in complex with FA hormones or TUG891 and G(i) or G(iq) trimers. Aromatic residues inside the GPR120 ligand pocket were responsible for recognizing different double-bond positions of these FAs and connect ligand recognition to distinct effector coupling. We also investigated synthetic ligand selectivity and the structural basis of missense single nucleotide polymorphisms. We reveal how GPR120 differentiates rigid double bonds and flexible single bonds and may facilitate rational drug design targeting to GPR120.
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Individual free fatty acids (FAs) play important roles in metabolic homeostasis, many through engagement with more than 40G protein-coupled receptors. Searching for receptors to sense beneficial omega-3 FAs of fish oil enabled the identification of GPR120, which is involved in a spectrum of metabolic diseases. Here, we report six cryo-electron microscopy structures of GPR120 in complex with FA hormones or TUG891 and G(i) or G(iq) trimers. Aromatic residues inside the GPR120 ligand pocket were responsible for recognizing different double-bond positions of these FAs and connect ligand recognition to distinct effector coupling. We also investigated synthetic ligand selectivity and the structural basis of missense single-nucleotide polymorphisms. We reveal how GPR120 differentiates rigid double bonds and flexible single bonds. The knowledge gleaned here may facilitate rational drug design targeting to GPR120.
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Unsaturated bond recognition leads to biased signal in a fatty acid receptor.,Mao C, Xiao P, Tao XN, Qin J, He QT, Zhang C, Guo SC, Du YQ, Chen LN, Shen DD, Yang ZS, Zhang HQ, Huang SM, He YH, Cheng J, Zhong YN, Shang P, Chen J, Zhang DL, Wang QL, Liu MX, Li GY, Guo Y, Xu HE, Wang C, Zhang C, Feng S, Yu X, Zhang Y, Sun JP Science. 2023 Mar 2:eadd6220. doi: 10.1126/science.add6220. PMID:36862765<ref>PMID:36862765</ref>
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Unsaturated bond recognition leads to biased signal in a fatty acid receptor.,Mao C, Xiao P, Tao XN, Qin J, He QT, Zhang C, Guo SC, Du YQ, Chen LN, Shen DD, Yang ZS, Zhang HQ, Huang SM, He YH, Cheng J, Zhong YN, Shang P, Chen J, Zhang DL, Wang QL, Liu MX, Li GY, Guo Y, Xu HE, Wang C, Zhang C, Feng S, Yu X, Zhang Y, Sun JP Science. 2023 Apr 7;380(6640):eadd6220. doi: 10.1126/science.add6220. Epub 2023 , Apr 7. PMID:36862765<ref>PMID:36862765</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

Current revision

Cryo-EM structure of the 9-hydroxystearic acid bound GPR120-Gi complex

PDB ID 8id3

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