7ewl
From Proteopedia
(Difference between revisions)
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<StructureSection load='7ewl' size='340' side='right'caption='[[7ewl]], [[Resolution|resolution]] 3.52Å' scene=''> | <StructureSection load='7ewl' size='340' side='right'caption='[[7ewl]], [[Resolution|resolution]] 3.52Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EWL FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.52Å</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=7ewl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ewl OCA], [https://pdbe.org/7ewl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ewl RCSB], [https://www.ebi.ac.uk/pdbsum/7ewl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ewl 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=7ewl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ewl OCA], [https://pdbe.org/7ewl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ewl RCSB], [https://www.ebi.ac.uk/pdbsum/7ewl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ewl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
- | == Function == | ||
- | [[https://www.uniprot.org/uniprot/GP158_HUMAN GP158_HUMAN]] Orphan receptor. | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | GPR158, a class C orphan GPCR, functions in cognition, stress-induced mood control, and synaptic development. Among class C GPCRs, GPR158 is unique as it lacks a Venus flytrap-fold ligand-binding domain and terminates Galphai/o protein signaling through the RGS7-Gbeta5 heterodimer. Here, we report the cryo-EM structures of GPR158 alone and in complex with one or two RGS7-Gbeta5 heterodimers. GPR158 dimerizes through Per-Arnt-Sim-fold extracellular and transmembrane (TM) domains connected by an epidermal growth factor-like linker. The TM domain (TMD) reflects both inactive and active states of other class C GPCRs: a compact intracellular TMD, conformations of the two intracellular loops (ICLs) and the TMD interface formed by TM4/5. The ICL2, ICL3, TM3, and first helix of the cytoplasmic coiled-coil provide a platform for the DHEX domain of one RGS7 and the second helix recruits another RGS7. The unique features of the RGS7-binding site underlie the selectivity of GPR158 for RGS7. | ||
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- | Structure of the class C orphan GPCR GPR158 in complex with RGS7-Gbeta5.,Jeong E, Kim Y, Jeong J, Cho Y Nat Commun. 2021 Nov 23;12(1):6805. doi: 10.1038/s41467-021-27147-1. PMID:34815401<ref>PMID:34815401</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 7ewl" style="background-color:#fffaf0;"></div> | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Cho | + | [[Category: Cho Y]] |
- | [[Category: Jeong | + | [[Category: Jeong E]] |
- | [[Category: Jeong | + | [[Category: Jeong J]] |
- | [[Category: Kim | + | [[Category: Kim Y]] |
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Current revision
cryo-EM structure of apo GPR158
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Categories: Large Structures | Cho Y | Jeong E | Jeong J | Kim Y