[Structural changes of lipid and thyroxine-binding protein zones of lipoprotein particles, containing human apolipoprotein A-1].
The relationship between temperature-induced structural changes in the lipid and protein thyroxine-binding zones of lipoprotein particles containing human apolipoprotein A-1 (apoA-1) as a sole protein component was studied using ESR with probes of two types--spin-labeled thyroxine and 5- or 16-doxylstearic acids. A structural rearrangement in the protein active site at 23-24 degrees was found. In the same temperature range, a dramatic change in the monolayer phospholipid ordered structure was observed. Based on these data, the localization of the apoA-1 thyroxine-binding site in the lipid phase as well as the possibility of regulation of the hormone binding process by changes in the protein-lipid interaction in lipoprotein particles are discussed.
Bovdeĭ
N A
NA
Sviridov
O V
OV
Kiselev
P A
PA
D016632:Apolipoprotein A-I / Q000032:analysis* / Q000737:chemistry; D001665:Binding Sites; D004578:Electron Spin Resonance Spectroscopy; D006801:Humans; D008055:Lipids / Q000737:chemistry*; D011487:Protein Conformation; D013113:Spin Labels; D013696:Temperature; D013975:Thyroxine-Binding Proteins / Q000737:chemistry*
D016632:Apolipoprotein A-I; D008055:Lipids; D013113:Spin Labels; D013975:Thyroxine-Binding Proteins