文章基本信息

标题：Apolipoprotein B-100: conservation of lipid-associating amphipathic secondary structural motifs in nine species of vertebrates
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作者：Jere P. Segrest ; Martin K. Jones ; Vinod K. Mishra 等
期刊名称：JLR Papers In Press
印刷版ISSN：0022-2275
电子版ISSN：1539-7262
出版年度：1998
卷号：39
期号：1
页码：85-102
语种：English
出版社：American Society for Biochemistry and Molecular Biology
摘要：Development of a computer program called LOCATE allowed us to show that human apolipoprotein B-100 is composed of five domains, NH₂-α₁-β₁-α₂-β₂-α₃-COOH, enriched, alternately, in amphipathic α helixes and amphipathic β 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 α helixes cluster in domains α₂ (between residues 2075 ± 25 and 2575 ± 25) and α₃ (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 β strands cluster in domains β₁ (approximately residues 827-2000) and β₂ (approximately residue 2571 to residue 4000 ± 50) in all species for which these regions have been sequenced, with conservation of several individual amphipathic β 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 β sheet-containing proteins. We conclude that four alternating lipid-associating domains, -β₁-α₂-β₂-α₃-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.
关键词：amphipc α helixes ; amphipathic β 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