7l0r: Difference between revisions
New page: '''Unreleased structure''' The entry 7l0r is ON HOLD Authors: Zhang, M., Gui, M., Wang, Z., Gorgulla, C., Yu, J.J., Wu, H., Sun, Z., Klenk, C., Merklinger, L., Morstein, L., Hagn, F., P... |
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==Structure of NTS-NTSR1-Gi complex in lipid nanodisc, noncanonical state, without AHD== | |||
<StructureSection load='7l0r' size='340' side='right'caption='[[7l0r]], [[Resolution|resolution]] 4.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7l0r]] 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=7L0R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7L0R 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]] 4.2Å</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=7l0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7l0r OCA], [https://pdbe.org/7l0r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7l0r RCSB], [https://www.ebi.ac.uk/pdbsum/7l0r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7l0r ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/NTR1_RAT NTR1_RAT] Receptor for the tridecapeptide neurotensin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. | |||
<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> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7l0r" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Neurotensin receptor|Neurotensin receptor]] | ||
[[Category: Hagn | *[[Transducin 3D structures|Transducin 3D structures]] | ||
[[Category: | == References == | ||
[[Category: Merklinger | <references/> | ||
[[Category: Morstein | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Rattus norvegicus]] | ||
[[Category: | [[Category: Brown A]] | ||
[[Category: | [[Category: Gorgulla C]] | ||
[[Category: Zhang | [[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 14:07, 23 October 2024
Structure of NTS-NTSR1-Gi complex in lipid nanodisc, noncanonical state, without AHDStructure of NTS-NTSR1-Gi complex in lipid nanodisc, noncanonical state, without AHD
Structural highlights
FunctionNTR1_RAT Receptor for the tridecapeptide neurotensin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. 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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