6e7k | pdb_00006e7k

Structure of the lipoprotein lipase GPIHBP1 complex that mediates plasma triglyceride hydrolysis

spinqualitylabelsall models 6e7k, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6e7k is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BMA, CA, FUC, NAG Activity: Lipoprotein lipase, with EC number 3.1.1.34 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease [LIPL_HUMAN] Hyperlipoproteinemia type 5;Familial lipoprotein lipase deficiency. The disease is caused by mutations affecting the gene represented in this entry. [HDBP1_HUMAN] Familial chylomicronemia syndrome. The disease is caused by mutations affecting the gene represented in this entry. Function [LIPL_HUMAN] The primary function of this lipase is the hydrolysis of triglycerides of circulating chylomicrons and very low density lipoproteins (VLDL) (PubMed:27578112). Binding to heparin sulfate proteogylcans at the cell surface is vital to the function. The apolipoprotein, APOC2, acts as a coactivator of LPL activity in the presence of lipids on the luminal surface of vascular endothelium (By similarity). [HDBP1_HUMAN] Plays a key role in the lipolytic processing of chylomicrons. Required for the transport of lipoprotein lipase LPL into the capillary lumen (By similarity).

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