8g2y: Difference between revisions
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==Cryo-EM structure of ADGRF1 coupled to miniGs/q== | |||
<StructureSection load='8g2y' size='340' side='right'caption='[[8g2y]], [[Resolution|resolution]] 3.44Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8g2y]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Lama_glama Lama glama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8G2Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8G2Y 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]] 3.44Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LPC:[1-MYRISTOYL-GLYCEROL-3-YL]PHOSPHONYLCHOLINE'>LPC</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=8g2y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8g2y OCA], [https://pdbe.org/8g2y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8g2y RCSB], [https://www.ebi.ac.uk/pdbsum/8g2y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8g2y ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Adhesion G Protein Coupled Receptors (aGPCRs) have evolved an activation mechanism to translate extracellular force into liberation of a tethered agonist (TA) to effect cell signalling. We report here that ADGRF1 can signal through all major G protein classes and identify the structural basis for a previously reported Galpha(q) preference by cryo-EM. Our structure shows that Galpha(q) preference in ADGRF1 may derive from tighter packing at the conserved F569 of the TA, altering contacts between TM helix I and VII, with a concurrent rearrangement of TM helix VII and helix VIII at the site of Galpha recruitment. Mutational studies of the interface and of contact residues within the 7TM domain identify residues critical for signalling, and suggest that Galpha(s) signalling is more sensitive to mutation of TA or binding site residues than Galpha(q). Our work advances the detailed molecular understanding of aGPCR TA activation, identifying features that potentially explain preferential signal modulation. | |||
Tethered agonist activated ADGRF1 structure and signalling analysis reveal basis for G protein coupling.,Jones DTD, Dates AN, Rawson SD, Burruss MM, Lipper CH, Blacklow SC Nat Commun. 2023 Apr 29;14(1):2490. doi: 10.1038/s41467-023-38083-7. PMID:37120430<ref>PMID:37120430</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8g2y" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Transducin 3D structures|Transducin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Lama glama]] | |||
[[Category: Large Structures]] | |||
[[Category: Blacklow S]] | |||
[[Category: Jones D]] | |||
[[Category: Rawson S]] | |||
Latest revision as of 12:38, 17 October 2024
Cryo-EM structure of ADGRF1 coupled to miniGs/qCryo-EM structure of ADGRF1 coupled to miniGs/q
Structural highlights
Publication Abstract from PubMedAdhesion G Protein Coupled Receptors (aGPCRs) have evolved an activation mechanism to translate extracellular force into liberation of a tethered agonist (TA) to effect cell signalling. We report here that ADGRF1 can signal through all major G protein classes and identify the structural basis for a previously reported Galpha(q) preference by cryo-EM. Our structure shows that Galpha(q) preference in ADGRF1 may derive from tighter packing at the conserved F569 of the TA, altering contacts between TM helix I and VII, with a concurrent rearrangement of TM helix VII and helix VIII at the site of Galpha recruitment. Mutational studies of the interface and of contact residues within the 7TM domain identify residues critical for signalling, and suggest that Galpha(s) signalling is more sensitive to mutation of TA or binding site residues than Galpha(q). Our work advances the detailed molecular understanding of aGPCR TA activation, identifying features that potentially explain preferential signal modulation. Tethered agonist activated ADGRF1 structure and signalling analysis reveal basis for G protein coupling.,Jones DTD, Dates AN, Rawson SD, Burruss MM, Lipper CH, Blacklow SC Nat Commun. 2023 Apr 29;14(1):2490. doi: 10.1038/s41467-023-38083-7. PMID:37120430[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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