7l0q: Difference between revisions
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==== | ==Structure of NTS-NTSR1-Gi complex in lipid nanodisc, canonical state, with AHD== | ||
<StructureSection load='7l0q' size='340' side='right'caption='[[7l0q]]' scene=''> | <StructureSection load='7l0q' size='340' side='right'caption='[[7l0q]], [[Resolution|resolution]] 4.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7l0q]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7L0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7L0Q FirstGlance]. <br> | ||
</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=7l0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7l0q OCA], [https://pdbe.org/7l0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7l0q RCSB], [https://www.ebi.ac.uk/pdbsum/7l0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7l0q ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.3Å</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=7l0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7l0q OCA], [https://pdbe.org/7l0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7l0q RCSB], [https://www.ebi.ac.uk/pdbsum/7l0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7l0q ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/GBG1_HUMAN GBG1_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. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
G-protein-coupled receptors (GPCRs) are the largest superfamily of transmembrane proteins and the targets of over 30% of currently marketed pharmaceuticals. Although several structures have been solved for GPCR-G protein complexes, few are in a lipid membrane environment. Here, we report cryo-EM structures of complexes of neurotensin, neurotensin receptor 1 and Galpha(i1)beta(1)gamma(1) in two conformational states, resolved to resolutions of 4.1 and 4.2 A. The structures, determined in a lipid bilayer without any stabilizing antibodies or nanobodies, reveal an extended network of protein-protein interactions at the GPCR-G protein interface as compared to structures obtained in detergent micelles. The findings show that the lipid membrane modulates the structure and dynamics of complex formation and provide a molecular explanation for the stronger interaction between GPCRs and G proteins in lipid bilayers. We propose an allosteric mechanism for GDP release, providing new insights into the activation of G proteins for downstream signaling. | |||
Cryo-EM structure of an activated GPCR-G protein complex in lipid nanodiscs.,Zhang M, Gui M, Wang ZF, Gorgulla C, Yu JJ, Wu H, Sun ZJ, Klenk C, Merklinger L, Morstein L, Hagn F, Pluckthun A, Brown A, Nasr ML, Wagner G Nat Struct Mol Biol. 2021 Mar;28(3):258-267. doi: 10.1038/s41594-020-00554-6. , Epub 2021 Feb 25. PMID:33633398<ref>PMID:33633398</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7l0q" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Neurotensin receptor|Neurotensin receptor]] | |||
*[[Transducin 3D structures|Transducin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Z | [[Category: Rattus norvegicus]] | ||
[[Category: Brown A]] | |||
[[Category: Gorgulla C]] | |||
[[Category: Gui M]] | |||
[[Category: Hagn F]] | |||
[[Category: Klenk C]] | |||
[[Category: Merklinger L]] | |||
[[Category: Morstein L]] | |||
[[Category: Nasr ML]] | |||
[[Category: Pluckthun A]] | |||
[[Category: Sun Z]] | |||
[[Category: Wagner G]] | |||
[[Category: Wang Z]] | |||
[[Category: Wu H]] | |||
[[Category: Yu JJ]] | |||
[[Category: Zhang M]] | |||
Latest revision as of 12:27, 9 October 2024
Structure of NTS-NTSR1-Gi complex in lipid nanodisc, canonical state, with AHDStructure of NTS-NTSR1-Gi complex in lipid nanodisc, canonical state, with AHD
Structural highlights
FunctionGBG1_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. Publication Abstract from PubMedG-protein-coupled receptors (GPCRs) are the largest superfamily of transmembrane proteins and the targets of over 30% of currently marketed pharmaceuticals. Although several structures have been solved for GPCR-G protein complexes, few are in a lipid membrane environment. Here, we report cryo-EM structures of complexes of neurotensin, neurotensin receptor 1 and Galpha(i1)beta(1)gamma(1) in two conformational states, resolved to resolutions of 4.1 and 4.2 A. The structures, determined in a lipid bilayer without any stabilizing antibodies or nanobodies, reveal an extended network of protein-protein interactions at the GPCR-G protein interface as compared to structures obtained in detergent micelles. The findings show that the lipid membrane modulates the structure and dynamics of complex formation and provide a molecular explanation for the stronger interaction between GPCRs and G proteins in lipid bilayers. We propose an allosteric mechanism for GDP release, providing new insights into the activation of G proteins for downstream signaling. Cryo-EM structure of an activated GPCR-G protein complex in lipid nanodiscs.,Zhang M, Gui M, Wang ZF, Gorgulla C, Yu JJ, Wu H, Sun ZJ, Klenk C, Merklinger L, Morstein L, Hagn F, Pluckthun A, Brown A, Nasr ML, Wagner G Nat Struct Mol Biol. 2021 Mar;28(3):258-267. doi: 10.1038/s41594-020-00554-6. , Epub 2021 Feb 25. PMID:33633398[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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