Apolipoprotein primary structure

Yang C Y, Gu ZW, Chong IS et al. The primary structure of human apolipoprotein A-IV. Biochim Biophys Acta. 1989, 1002 231-237. 

Given the widespread occurrence of sequences in apolipoproteins that evidently code for amphipathic helices, it is not surprising that many workers have attempted to identify possible secondary structural elements in apolipoproteins and to predict possible tertiary interactions and overall arrangements of secondary structure elements when these proteins are bound to lipids (Edelstein et al., 1979). Here we discuss models for apoA-1 and apoE-3 developed by Nolte and Atkinson (1992). These models resulted from an examination of the primary sequence of human plasma and apoA-1 and apoE-3 using a variety of approaches, and an integration of the resulting data into unihed predictions for the secondary structures of those molecules. 

The key structural features predicted for the amphipathic helix by the original model (Segrest et al., 1974) enabled three laboratories to study independently how amino acid variability determined the properties of the amphipathic helix (Kanellis et al., 1980 Fukushima et al., 1980 Sparrow et al., 1981). The strategy adapted by these investigators was based, not on the primary sequence of naturally occurring apolipoproteins, but on incorporating the periodicity of the secondary structural features of the amphipathic helix motif into the sequences of the peptide analogs. 

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