7eb2: Difference between revisions
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The | ==Cryo-EM structure of human GABA(B) receptor-Gi protein complex== | ||
<StructureSection load='7eb2' size='340' side='right'caption='[[7eb2]], [[Resolution|resolution]] 3.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7eb2]] is a 6 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=7EB2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EB2 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]] 3.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2C0:BACLOFEN'>2C0</scene>, <scene name='pdbligand=FN0:(3~{S})-5,7-di~{tert}-butyl-3-oxidanyl-3-(trifluoromethyl)-1-benzofuran-2-one'>FN0</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=7eb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7eb2 OCA], [https://pdbe.org/7eb2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7eb2 RCSB], [https://www.ebi.ac.uk/pdbsum/7eb2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7eb2 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/GNAI1_HUMAN GNAI1_HUMAN] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division.<ref>PMID:17635935</ref> <ref>PMID:17264214</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
G-protein-coupled receptors (GPCRs) have central roles in intercellular communication(1,2). Structural studies have revealed how GPCRs can activate G proteins. However, whether this mechanism is conserved among all classes of GPCR remains unknown. Here we report the structure of the class-C heterodimeric GABA(B) receptor, which is activated by the inhibitory transmitter GABA, in its active form complexed with G(i1) protein. We found that a single G protein interacts with the GB2 subunit of the GABA(B) receptor at a site that mainly involves intracellular loop 2 on the side of the transmembrane domain. This is in contrast to the G protein binding in a central cavity, as has been observed with other classes of GPCR. This binding mode results from the active form of the transmembrane domain of this GABA(B) receptor being different from that of other GPCRs, as it shows no outside movement of transmembrane helix 6. Our work also provides details of the inter- and intra-subunit changes that link agonist binding to G-protein activation in this heterodimeric complex. | |||
Structural basis of GABA(B) receptor-G(i) protein coupling.,Shen C, Mao C, Xu C, Jin N, Zhang H, Shen DD, Shen Q, Wang X, Hou T, Chen Z, Rondard P, Pin JP, Zhang Y, Liu J Nature. 2021 Jun;594(7864):594-598. doi: 10.1038/s41586-021-03507-1. Epub 2021 , Apr 28. PMID:33911284<ref>PMID:33911284</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7eb2" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[GABA receptor 3D structures|GABA receptor 3D structures]] | |||
*[[Transducin 3D structures|Transducin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Synthetic construct]] | |||
[[Category: Chen Z]] | |||
[[Category: Hou T]] | |||
[[Category: Jin N]] | |||
[[Category: Liu J]] | |||
[[Category: Mao C]] | |||
[[Category: Pin J]] | |||
[[Category: Rondard P]] | |||
[[Category: Shen C]] | |||
[[Category: Shen D]] | |||
[[Category: Shen Q]] | |||
[[Category: Wang X]] | |||
[[Category: Xu C]] | |||
[[Category: Zhang H]] | |||
[[Category: Zhang Y]] | |||
Latest revision as of 13:59, 23 October 2024
Cryo-EM structure of human GABA(B) receptor-Gi protein complexCryo-EM structure of human GABA(B) receptor-Gi protein complex
Structural highlights
FunctionGNAI1_HUMAN Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division.[1] [2] Publication Abstract from PubMedG-protein-coupled receptors (GPCRs) have central roles in intercellular communication(1,2). Structural studies have revealed how GPCRs can activate G proteins. However, whether this mechanism is conserved among all classes of GPCR remains unknown. Here we report the structure of the class-C heterodimeric GABA(B) receptor, which is activated by the inhibitory transmitter GABA, in its active form complexed with G(i1) protein. We found that a single G protein interacts with the GB2 subunit of the GABA(B) receptor at a site that mainly involves intracellular loop 2 on the side of the transmembrane domain. This is in contrast to the G protein binding in a central cavity, as has been observed with other classes of GPCR. This binding mode results from the active form of the transmembrane domain of this GABA(B) receptor being different from that of other GPCRs, as it shows no outside movement of transmembrane helix 6. Our work also provides details of the inter- and intra-subunit changes that link agonist binding to G-protein activation in this heterodimeric complex. Structural basis of GABA(B) receptor-G(i) protein coupling.,Shen C, Mao C, Xu C, Jin N, Zhang H, Shen DD, Shen Q, Wang X, Hou T, Chen Z, Rondard P, Pin JP, Zhang Y, Liu J Nature. 2021 Jun;594(7864):594-598. doi: 10.1038/s41586-021-03507-1. Epub 2021 , Apr 28. PMID:33911284[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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