Structural highlights
6ob0 is a 8 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , , , |
| 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).[1] [2] [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).
References
- ↑ Lutz EP, Merkel M, Kako Y, Melford K, Radner H, Breslow JL, Bensadoun A, Goldberg IJ. Heparin-binding defective lipoprotein lipase is unstable and causes abnormalities in lipid delivery to tissues. J Clin Invest. 2001 May;107(9):1183-92. doi: 10.1172/JCI11774. PMID:11342582 doi:http://dx.doi.org/10.1172/JCI11774
- ↑ Pingitore P, Lepore SM, Pirazzi C, Mancina RM, Motta BM, Valenti L, Berge KE, Retterstol K, Leren TP, Wiklund O, Romeo S. Identification and characterization of two novel mutations in the LPL gene causing type I hyperlipoproteinemia. J Clin Lipidol. 2016 Jul-Aug;10(4):816-823. doi: 10.1016/j.jacl.2016.02.015. Epub, 2016 Mar 10. PMID:27578112 doi:http://dx.doi.org/10.1016/j.jacl.2016.02.015
