1i5j

<StructureSection load='1i5j' size='340' side='right'caption='[[1i5j]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1i5j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I5J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I5J FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1i5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i5j OCA], [https://pdbe.org/1i5j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i5j RCSB], [https://www.ebi.ac.uk/pdbsum/1i5j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i5j ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/APOC2_HUMAN APOC2_HUMAN]] Defects in APOC2 are the cause of hyperlipoproteinemia type 1B (HLPP1B) [MIM:[https://omim.org/entry/207750 207750]]. It is an autosomal recessive trait characterized by hypertriglyceridemia, xanthomas, and increased risk of pancreatitis and early atherosclerosis.<ref>PMID:8323539</ref>

[[https://www.uniprot.org/uniprot/APOC2_HUMAN 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.

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== 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<ref>PMID:11331005</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1i5j" style="background-color:#fffaf0;"></div>

[[Category: Human]]

[[Category: Gooley, P R]]

[[Category: Hatters, D M]]

[[Category: Howlett, G J]]

[[Category: MacRaild, C A]]

[[Category: Protein-lipid interaction]]