1i5j | pdb_00001i5j

NMR STRUCTURE OF HUMAN APOLIPOPROTEIN C-II IN THE PRESENCE OF SDS

spinqualitylabelsall models 1i5j Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1i5j is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease APOC2_HUMAN Defects in APOC2 are the cause of hyperlipoproteinemia type 1B (HLPP1B) [MIM:207750. It is an autosomal recessive trait characterized by hypertriglyceridemia, xanthomas, and increased risk of pancreatitis and early atherosclerosis. Function APOC2_HUMAN Component of the very low density lipoprotein (VLDL) fraction in plasma, and is an activator of several triacylglycerol lipases. The association of APOC2 with plasma chylomicrons, VLDL, and HDL is reversible, a function of the secretion and catabolism of triglyceride-rich lipoproteins, and changes rapidly. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The structure and protein-detergent interactions of apolipoprotein C-II (apoC-II) in the presence of SDS micelles have been investigated using circular dichroism and heteronuclear NMR techniques applied to (15)N-labeled protein. Micellar SDS, a commonly used mimetic of the lipoprotein surface, inhibits the aggregation of apoC-II and induces a stable structure containing approximately 60% alpha-helix as determined by circular dichroism. NMR reveals the first 12 residues of apoC-II to be structurally heterogeneous and largely disordered, with the rest of the protein forming a predominantly helical structure. Three regions of helical conformation, residues 16-36, 50-56, and 63-77, are well-defined by NMR-derived constraints, with the intervening regions showing more loosely defined helical conformation. The structure of apoC-II is compared to that determined for other apolipoproteins in a similar environment. Our results shed light on the lipid interactions of apoC-II and its mechanism of lipoprotein lipase activation. NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate.,MacRaild CA, Hatters DM, Howlett GJ, Gooley PR Biochemistry. 2001 May 8;40(18):5414-21. PMID:11331005 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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