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8xjk

From Proteopedia

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Current revision (10:06, 17 October 2024) (edit) (undo)
 
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8xjk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xjk OCA], [https://pdbe.org/8xjk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xjk RCSB], [https://www.ebi.ac.uk/pdbsum/8xjk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xjk 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=8xjk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xjk OCA], [https://pdbe.org/8xjk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xjk RCSB], [https://www.ebi.ac.uk/pdbsum/8xjk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xjk ProSAT]</span></td></tr>
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</table>
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== Function ==
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<div style="background-color:#fffaf0;">
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[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>
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 8xjk" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Current revision

Cloprosetnol bound Prostaglandin F2-alpha receptor-Gq Protein Complex

PDB ID 8xjk

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OCA

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