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| | <StructureSection load='2e4z' size='340' side='right'caption='[[2e4z]], [[Resolution|resolution]] 3.30Å' scene=''> | | <StructureSection load='2e4z' size='340' side='right'caption='[[2e4z]], [[Resolution|resolution]] 3.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2e4z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E4Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2e4z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E4Z FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2e4u|2e4u]], [[2e4v|2e4v]], [[2e4w|2e4w]], [[2e4x|2e4x]], [[2e4y|2e4y]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</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=2e4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e4z OCA], [https://pdbe.org/2e4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e4z RCSB], [https://www.ebi.ac.uk/pdbsum/2e4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e4z 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=2e4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e4z OCA], [https://pdbe.org/2e4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e4z RCSB], [https://www.ebi.ac.uk/pdbsum/2e4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e4z ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/GRM7_RAT GRM7_RAT]] G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity.<ref>PMID:8145723</ref> <ref>PMID:8288585</ref>
| + | [https://www.uniprot.org/uniprot/GRM7_RAT GRM7_RAT] G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity.<ref>PMID:8145723</ref> <ref>PMID:8288585</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Jingami, H]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Morikawa, K]] | + | [[Category: Jingami H]] |
| - | [[Category: Muto, T]] | + | [[Category: Morikawa K]] |
| - | [[Category: Tsuchiya, D]] | + | [[Category: Muto T]] |
| - | [[Category: Central nerve system]]
| + | [[Category: Tsuchiya D]] |
| - | [[Category: G-protein-coupled receptor]]
| + | |
| - | [[Category: Neuron]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
GRM7_RAT G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Metabotropic glutamate receptors play major roles in the activation of excitatory synapses in the central nerve system. We determined the crystal structure of the entire extracellular region of the group II receptor and that of the ligand-binding region of the group III receptor. A comparison among groups I, II, and III provides the structural basis that could account for the discrimination of group-specific agonists. Furthermore, the structure of group II includes the cysteine-rich domain, which is tightly linked to the ligand-binding domain by a disulfide bridge, suggesting a potential role in transmitting a ligand-induced conformational change into the downstream transmembrane region. The structure also reveals the lateral interaction between the two cysteine-rich domains, which could stimulate clustering of the dimeric receptors on the cell surface. We propose a general activation mechanism of the dimeric receptor coupled with both ligand-binding and interprotomer rearrangements.
Structures of the extracellular regions of the group II/III metabotropic glutamate receptors.,Muto T, Tsuchiya D, Morikawa K, Jingami H Proc Natl Acad Sci U S A. 2007 Mar 6;104(10):3759-64. Epub 2007 Feb 26. PMID:17360426[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Saugstad JA, Kinzie JM, Mulvihill ER, Segerson TP, Westbrook GL. Cloning and expression of a new member of the L-2-amino-4-phosphonobutyric acid-sensitive class of metabotropic glutamate receptors. Mol Pharmacol. 1994 Mar;45(3):367-72. PMID:8145723
- ↑ Okamoto N, Hori S, Akazawa C, Hayashi Y, Shigemoto R, Mizuno N, Nakanishi S. Molecular characterization of a new metabotropic glutamate receptor mGluR7 coupled to inhibitory cyclic AMP signal transduction. J Biol Chem. 1994 Jan 14;269(2):1231-6. PMID:8288585
- ↑ Muto T, Tsuchiya D, Morikawa K, Jingami H. Structures of the extracellular regions of the group II/III metabotropic glutamate receptors. Proc Natl Acad Sci U S A. 2007 Mar 6;104(10):3759-64. Epub 2007 Feb 26. PMID:17360426
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