9p3t

Zebrafish TRPM5 with 5mM calcium and 0.5mM TPPO

spinqualitylabelsall models 9p3t, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9p3t is a 4 chain structure with sequence from Danio rerio. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3Å Ligands: A1CG5, CA, NAG, YUV, YUY Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TRPM5_DANRE Monovalent cation-selective ion channel activated by intracellular Ca(2+) in a voltage- and temperature-dependent manner. Mediates the transport of Na(+), K(+) and Cs(+) ions equally well. Activated directly by increase in intracellular Ca(2+), but is impermeable to it. The activation mechanism of TRPM5 involves a multistep process. TRPM5 activation involves ligand binding (i.e., tastant molecule, glucose stimulation) to Gq/G-protein coupled receptors (GPCR) and leads to the breakdown of phosphatidylinositol bisphosphate (PIP2) into diacylglycerol (DAG) and inositol trisphosphate (IP3), IP3 binds to its receptors in the endoplasmic reticulum and cause Ca(2+) release. Simultaneously with the intracellular Ca(2+) release, DAG activates the protein kinase C (PKC), which phosphorylates the TRPM5 channel. This phosphorylation combined with the bound Ca(2+), leads to a robust inward current allowing the entry of sodium ions (Na+) into the cell. This ion influx depolarizes the cell membrane, generating action potentials that propagate TRPM5 signals.[UniProtKB:Q9JJH7]GFP_AEQVI Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.

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