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Journal of Lipid Research, Vol 33, 141-166, Copyright © 1992 by Lipid Research, Inc.
JP Segrest, MK Jones, H De Loof, CG Brouillette, YV Venkatachalapathi and GM Anantharamaiah
Site-directed mutagenesis and other molecular biology-based techniques are
now available for probing the amphipathic alpha helix structural motif in
the exchangeable apolipoproteins. Here we survey the published literature
on lipid-binding and functional domains in apolipoproteins A- I, A-II,
A-IV, C-I, C-II, C-III, and E and compare these results with recently
developed computer methods for analysis of the location and properties of
amphipathic helixes. This comparison suggests that there are at least three
distinct classes of amphipathic helixes (classes A, Y, and G*) in the
exchangeable apolipoproteins whose distribution varies within and between
the seven apolipoproteins. This comparison further suggests that lipid
affinity resides largely in class A amphipathic helixes (Segrest, J. P., et
al. 1990. Proteins. 8: 103) and that variations in structure and/or numbers
of class A domains in individual apolipoproteins allow a range of lipid
affinities from high to low. The positions of the four alpha helixes
recently shown to form a 4-helix bundle globular structure in apoE (Wilson,
C., et al. 1991. Science. 252: 1817) correspond closely to the four
amino-terminal class G* amphipathic helixes of apoE identified by our
computer analysis. It is of particular interest, therefore, that all of the
exchangeable apolipoproteins except apoA-II and C-I, contain amphipathic
helixes of class G*. Additional implications of amphipathic helix
heterogeneity for the structure and function of the exchangeable
apolipoproteins will be discussed.
REVIEWS
The amphipathic helix in the exchangeable apolipoproteins: a review of secondary structure and function
Department of Medicine, UAB Medical Center, Birmingham 35294.
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