9y6p | pdb_00009y6p

Cryo-EM structure of PI(3,5)P2-bound full-length mouse TRPML2 channel in lipid nanodisc II

spinqualitylabelsall models 9y6p, resolution 3.88Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9y6p 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 3.88Å Ligands: EUJ Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MCLN2_MOUSE Nonselective cation channel probably playing a role in the regulation of membrane trafficking events. Acts as a Ca(2+)-permeable cation channel with inwardly rectifying activity (PubMed:19763610). May activate ARF6 and be involved in the trafficking of GPI-anchored cargo proteins to the cell surface via the ARF6-regulated recycling pathway (By similarity). May play a role in immune processes. In adaptive immunity, TRPML2 and TRPML1 may play redundant roles in the function of the specialized lysosomes of B cells (PubMed:17050035). In the innate immune response, may play a role in the regulation of chemokine secretion and macrophage migration (PubMed:26432893). Through a possible and probably tissue-specific heteromerization with MCOLN1 may be at least in part involved in many lysosome-dependent cellular events. Also functions as a Fe(2+) permeable channel (PubMed:18794901).[UniProtKB:Q8IZK6]

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