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Papers In Press, published online ahead of print May 30, 2008
J. Lipid Res., doi:10.1194/jlr.R800010-JLR200
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Pathology, Wake Forest University School of Medicine, Winston-Salem, NC 27040
Corresponding Author: msthomas{at}wfubmc.edu
The purpose of this review is to highlight recent advances towards the refinement of a 3-dimensional structure for lipid bound apoA-I on receombinant HDL. Recently, x-ray crystallography has yielded a new structure for full-length, lipid-free apoA-I. Although this approach has not yet been successful in solving the 3-dimensional structure of lipid-bound apoA-I, analysis of the X-ray structures has been of immense help in the interpretation of structural data obtained from other methods used to deduce structural information. Recent studies emphasize the use of mass spectrometry to unambiguously identify cross-linked peptides or to quantify solvent accessibility using hydrogen deuterium exchange. The combination of mass spectrometry, molecular modeling, molecular dynamic analysis and small angle X-ray diffraction has provided additional structural information on apoA-I folding that complements previous approaches.
Revised on May 19, 2008
Accepted on May 29, 2008
Three dimensional models of high density lipoprotein apoa-I:Implications for its assembly and function
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