Structure function relationship of the plasma apolipoproteins: a computational approach based on hydrophobicity characteristics.
Using different hydrophobicity analysis techniques we investigated the structure-function relationship of the different apolipoproteins. Lipid-binding domains were localized and within this class of protein domains, lecithin-cholesterol acyltransferase activating and non-activating amphipathic helices could be differentiated. A hydrophobic moment analysis of the apolipoprotein E sequence yielded interesting data concerning its receptor-binding and heparin binding characteristics. Finally we discuss the amphiphilic helical characteristics of certain domains of the apolipoprotein B sequence.
de Loof
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Department Clinical Biochemistry, AZ St-Jan, Brugge, Belgium.
D000595:Amino Acid Sequence; D001053:Apolipoproteins / Q000097:blood*; D001055:Apolipoproteins B / Q000378:metabolism; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004789:Enzyme Activation; D006493:Heparin / Q000378:metabolism; D006801:Humans; D050356:Lipid Metabolism; D007862:Phosphatidylcholine-Sterol O-Acyltransferase / Q000378:metabolism; D011956:Receptors, Cell Surface / Q000378:metabolism; D013329:Structure-Activity Relationship
D001053:Apolipoproteins; D001055:Apolipoproteins B; D011956:Receptors, Cell Surface; D006493:Heparin; D007862:Phosphatidylcholine-Sterol O-Acyltransferase