Title : Structural characterization of a low density lipoprotein receptor-active apolipoprotein E peptide, ApoE3-(126-183).

Pub. Date : 2000 Dec 8

PMID : 10986285






5 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 ApoE3-(126-183) efficiently transforms dimyristoylphosphatidylglycerol (DMPG) vesicles into peptide-lipid complexes. dimyristoylphosphatidylglycerol apolipoprotein E Homo sapiens
2 ApoE3-(126-183) efficiently transforms dimyristoylphosphatidylglycerol (DMPG) vesicles into peptide-lipid complexes. dimyristoylphosphatidylglycerol apolipoprotein E Homo sapiens
3 Far UV CD analysis of apoE3-(126-183).DMPG discs provided evidence that the peptide adopts a helical conformation. dimyristoylphosphatidylglycerol apolipoprotein E Homo sapiens
4 Competition binding experiments with (125)I-labeled low density lipoprotein (LDL) were conducted to assess the ability of apoE3-(126-183).DMPG complexes to bind to the LDL receptor. dimyristoylphosphatidylglycerol apolipoprotein E Homo sapiens
5 Both N-terminal apoE and the peptide, when complexed with DMPG, competed with (125)I-LDL for binding sites on the surface of cultured human skin fibroblasts. dimyristoylphosphatidylglycerol apolipoprotein E Homo sapiens