8ddw
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8ddw]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DDW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DDW FirstGlance]. <br> | <table><tr><td colspan='2'>[[8ddw]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DDW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DDW FirstGlance]. <br> | ||
| - | </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=8ddw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ddw OCA], [https://pdbe.org/8ddw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ddw RCSB], [https://www.ebi.ac.uk/pdbsum/8ddw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ddw ProSAT]</span></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]] 4.7Å</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=8ddw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ddw OCA], [https://pdbe.org/8ddw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ddw RCSB], [https://www.ebi.ac.uk/pdbsum/8ddw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ddw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | == | + | <div style="background-color:#fffaf0;"> |
| - | + | == Publication Abstract from PubMed == | |
| + | G-protein coupled receptors (GPCRs) govern the physiological response to stimuli by modulating the activity of downstream effectors, including ion channels. TRPM3 is an ion channel inhibited by GPCRs through direct interaction with G protein (Gbetagamma) released upon their activation. This GPCR-TRPM3 signaling pathway contributes to the analgesic effect of morphine. Here, we characterized Gbetagamma inhibition of TRPM3 using electrophysiology and single particle cryo-electron microscopy (cryo-EM). From electrophysiology, we obtained a half inhibition constant (IC50) of approximately 240 nM. Using cryo-EM, we determined structures of mouse TRPM3 expressed in human cells with and without Gbetagamma and with and without PIP(2), a lipid required for TRPM3 activity, at resolutions of 2.7-4.7 A. Gbetagamma-TRPM3 interfaces vary depending on PIP(2) occupancy; however, in all cases, Gbetagamma appears loosely attached to TRPM3. The IC50 in electrophysiology experiments raises the possibility that additional unknown factors may stabilize the TRPM3-Gbetagamma complex. | ||
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| + | Structural and functional analyses of a GPCR-inhibited ion channel TRPM3.,Zhao C, MacKinnon R Neuron. 2023 Jan 4;111(1):81-91.e7. doi: 10.1016/j.neuron.2022.10.002. Epub 2022 , Oct 24. PMID:36283409<ref>PMID:36283409</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8ddw" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Transducin 3D structures|Transducin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 05:21, 12 June 2024
cryo-EM structure of TRPM3 ion channel in complex with Gbg, tethered by ALFA-nanobody
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