Lipid-protein interactions in the plasma lipoproteins.
The purpose of this review has been to discuss new information about the mechanism of lipid and apoprotein interaction in the plasma lipoproteins. A special form of the amphipathic helix has been identified as a major structural element of the apolipoproteins sequenced to date. Evidence is reviewed concerning the role of the amphipathic helix in the binding to phospholipids. Several different models for the organization of the components of HDL, LDL and LP-X have evolved from extensive structural studies. Resolution of the differences among these models will require additional experimental testing. Verification of models based on the study of reconstituted HDL will require rigorous proof of native structure in these particles. A detailed description of the molecular organization of the lipid and protein constituents of the plasma lipoproteins is still lacking. Further structural and sequence studies with apoB and the "arginine-rich" protein are needed. Crystallization of an apoprotein or lipoprotein and determination of the three-dimensional structure would be a major achievement. With such further detailed structural information, it may then be possible to correlate changes in structure with determinants of metabolism.
D001053:Apolipoproteins / Q000097:blood / Q000378:metabolism; D001798:Blood Proteins / Q000032:analysis; D006801:Humans; D006838:Hydrocarbons / Q000378:metabolism; D008074:Lipoproteins / Q000097:blood*; D008244:Lysophosphatidylcholines / Q000378:metabolism; D008958:Models, Molecular; D010949:Plasma / Q000032:analysis*; D011485:Protein Binding; D013501:Surface-Active Agents / Q000378:metabolism
D001053:Apolipoproteins; D001798:Blood Proteins; D006838:Hydrocarbons; D008074:Lipoproteins; D008244:Lysophosphatidylcholines; D013501:Surface-Active Agents