8ddw | pdb_00008ddw

cryo-EM structure of TRPM3 ion channel in complex with Gbg, tethered by ALFA-nanobody

spinqualitylabelsall models 8ddw, resolution 4.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8ddw is a 10 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 4.7Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. , PMID:36283409 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transducin 3D structures

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