Template:STRUCTURE 1by6

Peptide of human apolipoprotein C-IIPeptide of human apolipoprotein C-II

Template:ABSTRACT PUBMED 10903476

DiseaseDisease

[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.[1]

FunctionFunction

[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.

About this StructureAbout this Structure

1by6 is a 1 chain structure. Full experimental information is available from OCA.

ReferenceReference

[xtra 1]

  1. Storjohann R, Rozek A, Sparrow JT, Cushley RJ. Structure of a biologically active fragment of human serum apolipoprotein C-II in the presence of sodium dodecyl sulfate and dodecylphosphocholine. Biochim Biophys Acta. 2000 Jul 19;1486(2-3):253-64. PMID:10903476
  1. Inadera H, Hibino A, Kobayashi J, Kanzaki T, Shirai K, Yukawa S, Saito Y, Yoshida S. A missense mutation (Trp 26-->Arg) in exon 3 of the apolipoprotein CII gene in a patient with apolipoprotein CII deficiency (apo CII-Wakayama). Biochem Biophys Res Commun. 1993 Jun 30;193(3):1174-83. PMID:8323539 doi:http://dx.doi.org/S0006-291X(83)71749-3

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OCA