8thr

Structure of the human vesicular monoamine transporter 2 (VMAT2) bound to tetrabenazine in an occluded conformation

spinqualitylabelsall models 8thr, resolution 3.12Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8thr is a 1 chain structure with sequence from Aequorea victoria, Homo sapiens and Vicugna pacos. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.12Å Ligands: EBZ Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease VMAT2_HUMAN Brain dopamine-serotonin vesicular transport disease. The disease is caused by variants affecting the gene represented in this entry. Function VMAT2_HUMAN Electrogenic antiporter that exchanges one cationic monoamine with two intravesicular protons across the membrane of secretory and synaptic vesicles. Uses the electrochemical proton gradient established by the V-type proton-pump ATPase to accumulate high concentrations of monoamines inside the vesicles prior to their release via exocytosis. Transports a variety of catecholamines such as dopamine, adrenaline and noradrenaline, histamine, and indolamines such as serotonin (PubMed:8643547, PubMed:23363473). Regulates the transvesicular monoaminergic gradient that determines the quantal size. Mediates somatodendritic dopamine release in hippocampal neurons, likely as part of a regulated secretory pathway that integrates retrograde synaptic signals (By similarity). Acts as a primary transporter for striatal dopamine loading ensuring impulse-dependent release of dopamine at the synaptic cleft (By similarity). Responsible for histamine and serotonin storage and subsequent corelease from mast cell granules (PubMed:8860238) (By similarity).[UniProtKB:Q01827][UniProtKB:Q8BRU6]

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