7f23: Difference between revisions
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==Cryo-EM structure of the GTP-bound dopamine receptor 1 and mini-Gs complex with Nb35== | |||
<StructureSection load='7f23' size='340' side='right'caption='[[7f23]], [[Resolution|resolution]] 3.58Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7f23]] 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=7F23 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7F23 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]] 3.58Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=LDP:L-DOPAMINE'>LDP</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=7f23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7f23 OCA], [https://pdbe.org/7f23 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7f23 RCSB], [https://www.ebi.ac.uk/pdbsum/7f23 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7f23 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
G protein-coupled receptors (GPCRs) comprise the largest family of membrane receptors and are the most important drug targets. An agonist-bound GPCR engages heterotrimeric G proteins and triggers the exchange of guanosine diphosphate (GDP) with guanosine triphosphate (GTP) to promote G protein activation. A complete understanding of molecular mechanisms of G protein activation has been hindered by a lack of structural information of GPCR-G protein complex in nucleotide-bound states. Here, we report the cryo-EM structures of the D1 dopamine receptor and mini-G(s) complex in the nucleotide-free and nucleotide-bound states. These structures reveal major conformational changes in Galpha such as structural rearrangements of the carboxyl- and amino-terminal alpha helices that account for the release of GDP and the GTP-dependent dissociation of Galpha from Gbetagamma subunits. As validated by biochemical and cellular signaling studies, our structures shed light into the molecular basis of the entire signaling events of GPCR-mediated G protein activation. | |||
Structural insights into G protein activation by D1 dopamine receptor.,Teng X, Chen S, Wang Q, Chen Z, Wang X, Huang N, Zheng S Sci Adv. 2022 Jun 10;8(23):eabo4158. doi: 10.1126/sciadv.abo4158. Epub 2022 Jun , 10. PMID:35687690<ref>PMID:35687690</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7f23" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Dopamine receptor 3D structures|Dopamine receptor 3D structures]] | |||
*[[Transducin 3D structures|Transducin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Synthetic construct]] | |||
[[Category: Xiao T]] | |||
[[Category: Zheng S]] | |||
Latest revision as of 11:43, 17 October 2024
Cryo-EM structure of the GTP-bound dopamine receptor 1 and mini-Gs complex with Nb35Cryo-EM structure of the GTP-bound dopamine receptor 1 and mini-Gs complex with Nb35
Structural highlights
Publication Abstract from PubMedG protein-coupled receptors (GPCRs) comprise the largest family of membrane receptors and are the most important drug targets. An agonist-bound GPCR engages heterotrimeric G proteins and triggers the exchange of guanosine diphosphate (GDP) with guanosine triphosphate (GTP) to promote G protein activation. A complete understanding of molecular mechanisms of G protein activation has been hindered by a lack of structural information of GPCR-G protein complex in nucleotide-bound states. Here, we report the cryo-EM structures of the D1 dopamine receptor and mini-G(s) complex in the nucleotide-free and nucleotide-bound states. These structures reveal major conformational changes in Galpha such as structural rearrangements of the carboxyl- and amino-terminal alpha helices that account for the release of GDP and the GTP-dependent dissociation of Galpha from Gbetagamma subunits. As validated by biochemical and cellular signaling studies, our structures shed light into the molecular basis of the entire signaling events of GPCR-mediated G protein activation. Structural insights into G protein activation by D1 dopamine receptor.,Teng X, Chen S, Wang Q, Chen Z, Wang X, Huang N, Zheng S Sci Adv. 2022 Jun 10;8(23):eabo4158. doi: 10.1126/sciadv.abo4158. Epub 2022 Jun , 10. PMID:35687690[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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