8xjm
From Proteopedia
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<table><tr><td colspan='2'>[[8xjm]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8XJM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8XJM FirstGlance]. <br> | <table><tr><td colspan='2'>[[8xjm]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8XJM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8XJM 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]] 2.85Å</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]] 2.85Å</td></tr> | ||
| - | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7WT:Z-7-[( | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7WT:(~{Z})-7-[(1~{R},2~{R},3~{R},5~{S})-3,5-bis(oxidanyl)-2-[(3~{R})-3-oxidanyl-5-phenyl-pentyl]cyclopentyl]hept-5-enoic+acid'>7WT</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=8xjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xjm OCA], [https://pdbe.org/8xjm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xjm RCSB], [https://www.ebi.ac.uk/pdbsum/8xjm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xjm 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=8xjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xjm OCA], [https://pdbe.org/8xjm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xjm RCSB], [https://www.ebi.ac.uk/pdbsum/8xjm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xjm 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> | [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 == | ||
| + | Prostaglandin F(2alpha) (PGF(2alpha)) and thromboxane A(2) (TXA(2)) are endogenous arachidonic acid metabolites, modulating diverse physiological processes including inflammation and cardiovascular homeostasis through activating PGF(2alpha) receptor (FP) and TXA(2) receptor (TP). Ligands targeting FP and TP have demonstrated efficacy in treating conditions like glaucoma and cardiovascular diseases in humans, as well as reproductive-related diseases in animals. Here, we present five cryoelectron microscopy structures illustrating FP and TP in complex with G(q) and bound to PGF(2alpha) (endogenous ligand), latanoprost acid (a clinical drug), and two other synthetic agonists. Combined with mutational and functional studies, these structures reveal not only structural features for the specific recognition of endogenous ligands and attainment of receptor selectivity of FP and TP but also the common mechanisms of receptor activation and G(q) protein coupling. The findings may enrich our knowledge of ligand recognition and signal transduction of the prostanoid receptor family and facilitate rational ligand design toward these two receptors. | ||
| + | |||
| + | Structural basis for ligand recognition and activation of the prostanoid receptors.,Li X, Zhang X, Wen X, Zhang D, Qu C, Miao X, Zhang W, Zhang R, Liu G, Xiao P, Sun JP, Gong W Cell Rep. 2024 Mar 26;43(3):113893. doi: 10.1016/j.celrep.2024.113893. Epub 2024 , Mar 5. PMID:38446662<ref>PMID:38446662</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8xjm" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Latanoprost acid bound Prostaglandin F2-alpha receptor-Gq Protein Complex
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Categories: Homo sapiens | Large Structures | Synthetic construct | Gong W | Li X | Liu G | Zhang X
