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The Journal of Lipid Research, Vol. 39, 85-102, January 1998
Copyright © 1998 by Lipid Research, Inc.

Original Article

Apolipoprotein B-100: conservation of lipid-associating amphipathic secondary structural motifs in nine species of vertebrates

Correspondence to: Jere P. Segrest.

Development of a computer program called LOCATE allowed us to show that human apolipoprotein B-100 is composed of five domains, NH₂-₁-ß₁-₂-ß₂-₃-COOH, enriched, alternately, in amphipathic helixes and amphipathic ß strands. Using updated versions of this program, here we compare the complete sequence of human apolipoprotein B-100 with partial sequences from eight additional species of vertebrates (chicken, frog, hamster, monkey, mouse, pig, rat, and rabbit). The lipid-associating amphipathic helixes cluster in domains ₂ (between residues 2075 ± 25 and 2575 ± 25) and ₃ (between residues 4100 ± 100 and 4550 ± 50) in all species for which those regions have been sequenced but with little conservation of individual helixes. Lipid-associating amphipathic ß strands cluster in domains ß₁ (approximately residues 827-2000) and ß₂ (approximately residue 2571 to residue 4000 ± 50) in all species for which these regions have been sequenced, with conservation of several individual amphipathic ß strands. Hydrophobic segments are present in apolipoprotein B-100 sequences of all nine species but the frequency of occurrence is no greater than generally found in ß sheet-containing proteins.

We conclude that four alternating lipid-associating domains, - ß₁-₂-ß₂-₃-COOH, are common supramolecular features of apolipoprotein B-100 in nine vertebrate species.— Segrest, J. P., M. K. Jones, V. K. Mishra, V. Pierotti, S. H. Young, J. Borén, T. L. Innerarity, and N. Dashti. Apolipoprotein B-100: conservation of lipid-associating amphipathic secondary structural motifs in nine species of vertebrates. J. Lipid Res. 1998. 39: 85–102.

Supplementary key words: amphipathic helixes, amphipathic ß strands, hydrophobic amino acid sequences, plasma lipoproteins, computer analysis of amphipathic motifs, low density lipoprotein, protein homology, computer program LOCATE, amphipathic domains, protein–lipid interactions

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