6n4x: Difference between revisions
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<StructureSection load='6n4x' size='340' side='right'caption='[[6n4x]], [[Resolution|resolution]] 4.00Å' scene=''> | <StructureSection load='6n4x' size='340' side='right'caption='[[6n4x]], [[Resolution|resolution]] 4.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6n4x]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6n4x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N4X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6N4X FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6n4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n4x OCA], [https://pdbe.org/6n4x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6n4x RCSB], [https://www.ebi.ac.uk/pdbsum/6n4x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6n4x ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Feng | [[Category: Feng D]] | ||
[[Category: Hu | [[Category: Hu H]] | ||
[[Category: Kobilka | [[Category: Kobilka BK]] | ||
[[Category: Koehl | [[Category: Koehl A]] | ||
[[Category: Mathiesen | [[Category: Mathiesen JM]] | ||
[[Category: Skiniotis | [[Category: Skiniotis GS]] | ||
[[Category: Sun | [[Category: Sun B]] | ||
[[Category: Weis | [[Category: Weis WI]] | ||
Latest revision as of 09:45, 11 October 2023
Metabotropic Glutamate Receptor 5 Apo Form Ligand Binding DomainMetabotropic Glutamate Receptor 5 Apo Form Ligand Binding Domain
Structural highlights
FunctionGRM5_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. Publication Abstract from PubMedMetabotropic glutamate receptors are family C G-protein-coupled receptors. They form obligate dimers and possess extracellular ligand-binding Venus flytrap domains, which are linked by cysteine-rich domains to their 7-transmembrane domains. Spectroscopic studies show that signalling is a dynamic process, in which large-scale conformational changes underlie the transmission of signals from the extracellular Venus flytraps to the G protein-coupling domains-the 7-transmembrane domains-in the membrane. Here, using a combination of X-ray crystallography, cryo-electron microscopy and signalling studies, we present a structural framework for the activation mechanism of metabotropic glutamate receptor subtype 5. Our results show that agonist binding at the Venus flytraps leads to a compaction of the intersubunit dimer interface, thereby bringing the cysteine-rich domains into close proximity. Interactions between the cysteine-rich domains and the second extracellular loops of the receptor enable the rigid-body repositioning of the 7-transmembrane domains, which come into contact with each other to initiate signalling. Structural insights into the activation of metabotropic glutamate receptors.,Koehl A, Hu H, Feng D, Sun B, Zhang Y, Robertson MJ, Chu M, Kobilka TS, Laermans T, Steyaert J, Tarrasch J, Dutta S, Fonseca R, Weis WI, Mathiesen JM, Skiniotis G, Kobilka BK Nature. 2019 Feb;566(7742):79-84. doi: 10.1038/s41586-019-0881-4. Epub 2019 Jan, 23. PMID:30675062[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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