7y24
From Proteopedia
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(New page: '''Unreleased structure''' The entry 7y24 is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of the octreotide-bound SSTR2-miniGo-scFv16 complex== | |
| + | <StructureSection load='7y24' size='340' side='right'caption='[[7y24]], [[Resolution|resolution]] 3.25Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7y24]] is a 6 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=7Y24 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Y24 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]] 3.25Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DPN:D-PHENYLALANINE'>DPN</scene>, <scene name='pdbligand=DTR:D-TRYPTOPHAN'>DTR</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=7y24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7y24 OCA], [https://pdbe.org/7y24 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7y24 RCSB], [https://www.ebi.ac.uk/pdbsum/7y24 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7y24 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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 == | ||
| + | G protein-coupled receptors (GPCRs) modulate every aspect of physiological functions mainly through activating heterotrimeric G proteins. A majority of GPCRs promiscuously couple to multiple G protein subtypes. Here we validate that in addition to the well-known G(i/o) pathway, somatostatin receptor 2 and 5 (SSTR2 and SSTR5) couple to the G(q/11) pathway and show that smaller ligands preferentially activate the G(i/o) pathway. We further determined cryo-electron microscopy structures of the SSTR2âG(o) and SSTR2âG(q) complexes bound to octreotide and SST-14. Structural and functional analysis revealed that G protein selectivity of SSTRs is not only determined by structural elements in the receptor-G protein interface, but also by the conformation of the agonist-binding pocket. Accordingly, smaller ligands fail to stabilize a broader agonist-binding pocket of SSTRs that is required for efficient G(q/11) coupling but not G(i/o) coupling. Our studies facilitate the design of drugs with selective G protein signaling to improve therapeutic efficacy. | ||
| - | + | Molecular basis for the selective G protein signaling of somatostatin receptors.,Chen S, Teng X, Zheng S Nat Chem Biol. 2023 Feb;19(2):133-140. doi: 10.1038/s41589-022-01130-3. Epub 2022 , Sep 22. PMID:36138141<ref>PMID:36138141</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7y24" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Transducin 3D structures|Transducin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chen S]] | ||
| + | [[Category: Zheng S]] | ||
Current revision
Cryo-EM structure of the octreotide-bound SSTR2-miniGo-scFv16 complex
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