Apolipoprotein structural organization in high density lipoproteins: belts, bundles, hinges and hairpins.
OBJECTIVE
To summarize recent advances towards an understanding of the three-dimensional structures of the apolipoprotein components of HDL with a specific focus on high resolution models of apolipoprotein A-I.


RESULTS
Since the primary sequence was first reported, various models have been advanced for the structure of apolipoprotein A-I, the major protein constituent of HDL, in its lipid-free and lipid-bound forms. Unfortunately, the generation of experimental data capable of distinguishing among the competing models has lagged far behind. However, recent experimental strategies, including X-ray crystallography, applications of resonance energy transfer and mass spectrometry, have combined with sophisticated theoretical approaches to develop three-dimensional structural models of apolipoprotein A-I with previously unavailable resolution.


CONCLUSIONS
The recent synergy of sophisticated computer modeling techniques with hard experimental data has generated new models for apolipoprotein A-I in certain subclasses of HDL produced in vitro. The challenge now is to adapt and test these models in the more complex forms of HDL isolated directly from human plasma.
Davidson
W Sean
WS
Department of Pathology and Laboratory Medicine, University of Cincinnati, Cincinnati, Ohio 45237-0507, USA. sean.davidson@uc.edu
Silva
R A Gangani D
RA
D016632:Apolipoprotein A-I / Q000737:chemistry* / Q000502:physiology*; D008076:Cholesterol, HDL / Q000737:chemistry*; D018360:Crystallography, X-Ray; D006801:Humans; D008956:Models, Chemical; D011487:Protein Conformation
D016632:Apolipoprotein A-I; D008076:Cholesterol, HDL