9b28

Cryo-EM structure of the mouse TRPM3 alpha 2 channel in complex with primidone

spinqualitylabelsall models 9b28, resolution 3.24Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9b28 is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.24Å Ligands: 6OU, A1AIA, Y01 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TRPM3_MOUSE Constitutively active, non-selective divalent cation-conducting channel that is permeable to Ca(2+), Mn(2+), and Mg(2+), with a high permeability for Ca(2+) (PubMed:15824111, PubMed:20401728, PubMed:32780479). However, can be enhanced by increasing temperature and by ligands, including the endogenous neurosteroid pregnenolone sulfate and sphingosine-1 and suppressed by intracellular Mg(2+) (PubMed:20401728, PubMed:21555074). Implicated in a variety of cellular processes, including insulin/peptide secretion, vascular constriction and dilation, noxious heat sensing, inflammatory and spontaneous pain sensitivity (PubMed:21555074, PubMed:30853321, PubMed:33478988). In neurons of the dorsal root ganglia, functions as thermosensitive channel for the detection of noxious heat and spontaneous pain (PubMed:21555074, PubMed:33478988). Suggested to function as an ionotropic steroid receptor in beta-cell, indeed pregnenolone sulfate leads to Ca(2+) influx and enhanced insulin secretion (PubMed:18978782). Mediates Zn(2+) uptake into the lumen of pancreatic beta cell secretory granules, thereby regulating insulin secretion (PubMed:20401728). Forms heteromultimeric ion channels with TRPM1 which are permeable for Ca(2+) and Zn(2+) ions (By similarity). Exists as multiple splice variants which differ significantly in their biophysical properties (PubMed:15824111, PubMed:22961981).[UniProtKB:Q9HCF6] Displays strongly reduced permeability for divalent cations and high selectivity toward monovalent cations. No channel activity. No channel activity.

Proteopedia Page Contributors and Editors (what is this?)

OCA