7fd8: Difference between revisions

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<StructureSection load='7fd8' size='340' side='right'caption='[[7fd8]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
<StructureSection load='7fd8' size='340' side='right'caption='[[7fd8]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7fd8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7FD8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7FD8 FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7FD8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7FD8 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=QUS:(S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC+ACID'>QUS</scene>, <scene name='pdbligand=Y01:CHOLESTEROL+HEMISUCCINATE'>Y01</scene></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]] 3.8&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7p2l|7p2l]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=QUS:(S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC+ACID'>QUS</scene>, <scene name='pdbligand=Y01:CHOLESTEROL+HEMISUCCINATE'>Y01</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GRM5, GPRC1E, MGLUR5 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=7fd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7fd8 OCA], [https://pdbe.org/7fd8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7fd8 RCSB], [https://www.ebi.ac.uk/pdbsum/7fd8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7fd8 ProSAT]</span></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=7fd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7fd8 OCA], [https://pdbe.org/7fd8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7fd8 RCSB], [https://www.ebi.ac.uk/pdbsum/7fd8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7fd8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/GRM5_HUMAN GRM5_HUMAN]] Receptor for glutamate. The activity of this receptor is mediated by a G-protein that activates a phosphatidylinositol-calcium second messenger system and generates a calcium-activated chloride current.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Metabotropic glutamate receptors (mGluRs) are dimeric G-protein-coupled receptors activated by the main excitatory neurotransmitter, L-glutamate. mGluR activation by agonists binding in the venus flytrap domain is regulated by positive (PAM) or negative (NAM) allosteric modulators binding to the 7-transmembrane domain (7TM). We report the cryo-electron microscopy structures of fully inactive and intermediate-active conformations of mGlu5 receptor bound to an antagonist and a NAM or an agonist and a PAM, respectively, as well as the crystal structure of the 7TM bound to a photoswitchable NAM. The agonist induces a large movement between the subunits, bringing the 7TMs together and stabilizing a 7TM conformation structurally similar to the inactive state. Using functional approaches, we demonstrate that the PAM stabilizes a 7TM active conformation independent of the conformational changes induced by agonists, representing an alternative mode of mGlu activation. These findings provide a structural basis for different mGluR activation modes.


Agonists and allosteric modulators promote signaling from different metabotropic glutamate receptor 5 conformations.,Nasrallah C, Cannone G, Briot J, Rottier K, Berizzi AE, Huang CY, Quast RB, Hoh F, Baneres JL, Malhaire F, Berto L, Dumazer A, Font-Ingles J, Gomez-Santacana X, Catena J, Kniazeff J, Goudet C, Llebaria A, Pin JP, Vinothkumar KR, Lebon G Cell Rep. 2021 Aug 31;36(9):109648. doi: 10.1016/j.celrep.2021.109648. PMID:34469715<ref>PMID:34469715</ref>
==See Also==
 
*[[Metabotropic glutamate receptor 3D structures|Metabotropic glutamate receptor 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7fd8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cannone, G]]
[[Category: Cannone G]]
[[Category: Lebon, G]]
[[Category: Lebon G]]
[[Category: Vinothkumar, K R]]
[[Category: Vinothkumar KR]]
[[Category: G protein coupled receptor]]
[[Category: Membrane protein]]
[[Category: Signal transduction]]

Latest revision as of 11:29, 30 October 2024

Thermostabilised full length human mGluR5-5M bound with L-quisqualic acid

7fd8, resolution 3.80Å

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