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

Journal of Lipid Research

Volumn 39, Issue 1, 1998, Pages 85-102

  Segrest, Jere P ^a   Jones, Martin K ^a   Mishra, Vinod K ^a   Pierotti, Vincenzo ^b   Young, Stephen H ^b   Borén, Jan ^b   Innerarity, Thomas L ^b   Dashti, Nassrin ^a  

^a UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

^b GLADSTONE INSTITUTE OF CARDIOVASCULAR DISEASE   (United States)

Author keywords

Amphipathic helixes; Amphipathic strands; Amphipathic domains; Computer analysis of amphipathic motifs; Computer program LOCATE; Hydrophobic amino acid sequences; Low density lipoprotein; Plasma lipoproteins; Protein homology; Protein lipid interactions

Indexed keywords

APOLIPOPROTEIN B100;

AMINO ACID SEQUENCE; ARTICLE; COMPUTER PROGRAM; HUMAN; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN LIPID INTERACTION; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; SPECIES DIFFERENCE; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; ANURA; APOLIPOPROTEIN B-100; APOLIPOPROTEINS B; BINDING SITES; CHICKENS; CRICETINAE; HAPLORHINI; HUMANS; LIPID METABOLISM; MICE; PROTEIN STRUCTURE, SECONDARY; RABBITS; RATS; RECEPTORS, LDL; SEQUENCE ALIGNMENT; SOFTWARE; SWINE;

EID: 0031882254     PISSN: 00222275     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (26)

1. Segrest, J. P., R. L. Jackson, J. D. Morrisett, and A. M. Gotto. 1974. A molecular theory of lipid-protein interactions in the plasma lipoproteins. FEBS Lett. 38: 247-253.
2. Segrest, J. P., D. W. Garber, C. G. Brouillette, S. C. Harvey, and G. M. Anantharamaiah. 1994. The amphipathic α helix: a multifunctional structural motif in plasma apolipoproteins. Adv. Protein Chem. 45: 303-369.
3. Segrest, J. P., H. De Loof, J. G. Dohlman, C. G. Brouillette, and G. M. Anantharamaiah. 1990. The amphipathic helix motif: classes and properlies. Proteins: Struct. Funct. Genet. 7: 1-15.
4. Segrest, J. P., M. K. Jones, H. De Loof, C. G. Brouillette, Y. V. Venkatachalapathi, and G. M. Anantharamaiah. 1992. The amphipathic helix in the exchangeable apolipoproteins: a review. J. Lipid Res. 33: 141-166.
5. Wilson, C., M. R. Wardell, K. H. Weisgraber, R. W. Mahley, and D. A. Agard. 1991. The three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E. Science. 252: 1817-1822.
6. Segrest, J. P., M. K. Jones, V. K. Mishra, G. M. Anantharamaiah, and D. W. Garber. 1994. Apolipoprotein B-100 has a pentapartite structure composed of three amphipathic a helical domains alternating with two amphipathic β strand domains: detection by the computer program LOCATE. Artmoscler. Thromb. 14: 1674-1685.
7. Jones, M. K., G. M. Anantharamaiah, and J. P. Segrest. 1992. Computer programs to identify and classify amphipathic a helical domains. J. Lipid Res. 33: 287-296.
8. Engelman, D. M., T. A., Steitz, and A. Goldman. 1986. Identifying transbilayer helices in amino acid sequences of membrane proteins. Annu. Rev. Biophys. Biophys.Chem. 15: 321-353.
9. Palgunachari, M. N., V. K. Mishra, S. Lund-Katz, M. C. Phillips, S. O. Adeyeye, S. Alluri, G. M. Anantharamaiah, and J. P. Segrest. 1996. Only the two end helixes of eight tandem amphipathic helical domains of human apoA-I have significant lipid affinity: implications for HDL assembly. Arterioscler. Thmmb. Vasc. Biol. 16: 328-338.
10. Jacobs, R. E., and S. H. White. 1989. The nature of hydrophobic binding of small peptides at the bilayer interface: implications for the insertion of transbilayer helices. Biochemistry. 28: 3421-3437.
11. Schuler, G. D., S. F. Altschul, and D. J. Lipman. 1991. A workbench for multiple alignment construction and analysis. Proteins Struct. Funct. Genet. 9: 180-190.
12. Lawrence, C. E., S. F. Altschul, M. S. Boguski, J. S. Liu, A. F. Neuwald, and J. C. Wootton. 1993. Detecting subtle sequence signals: a Gibbs sampling strategy for multiple alignment. Science. 262: 208-214.
13. Yang, C-Y., Z-W. Gu, S. A. Weng, T. W. Kim, S-H. Chen, H. J. Pownall, P. M. Sharp, S. W. Liu, W. H. Li, A. M. Gotto, Jr., and L. Chan. 1989. Structure of apolipoprotein B-100 of human low density lipoproteins. Arterioscler. Thromb. 9: 96-108.
14. De Loof, H., M. Rosseneu, C. Y. Yang, W. H. Li, A. M. Gotto, and L. Chan. 1987. Human apolipoprotein B: analysis of internal repeats and homology with other apolipoproteins. J. Lipid Res. 28: 1455-1465.
15. Nolte, R. T. 1994. Structural analysis of the human apolipoproteins: an integrated approach utilizing physical and computational methods. Thesis Dissertation. Boston University.
16. Gotto, A. M., R. I. Levy, and D. S. Fredrickson. 1968. Observations on the conformation of human beta lipoprotein: evidence for the occurrence of beta structure. Biochemistry. 60: 1436-1441.
17. Scann, A., and R. Hirz. 1968. Human serum low-density lipoprotein protein: its conformation studied by circular dichroism. Nature. 218: 200-201.
18. Chen, G., and J. P. Kane. 1979. Secondary structure in very low density and intermediate density lipoproteins of human serum. J. Lipid Res. 20: 481-488.
19. Walsh, M. T., and D. Atkinson. 1983. Solubilization of low-density lipoprotein with sodium deoxycholate and recombination of apoprotein B with dimyristoylphosphatidylcholine. Biochemistry. 22: 3170-3178.
20. Goormaghtigh, E., V. Cabianx, J. De Meutter, M. Rosseneu, and J. M. Ruysschaert. 1993. Secondary structure of the particle associating domain of apolipoprotein B-100 in low-density lipoprotein by attenuated total reflection infrared spectroscopy. Biochemistry. 32: 6104-6110.
21. Osterman, D., R. Mora, F. J. Kézdy, E. T. Kaiser, and S. C. Meredith. 1984. A synthetic amphiphilic β-strand trideca-peptide: a model for apolipoprotein B. J. Am. Chem. Soc. 106: 6845-6847.
22. Young, S. D., S. T. Hubi, R. S. Smith, S. M. Snyder, and J. F. Terdiman. 1990. Familial dysbetalipoproteinemia caused by a mutation in the apolipoprotein B gene that results in a truncated species of apolipoprotein B (B-31): a unique mutation that helps to define the portion of the apolipoprotein B molecule required for the formation of buoyant, triglyceride-rich lipoproteins. J. Clin. Invest. 85: 933-942.
23. Yao, Z., B. D. Blackhart, M. F. Linton, S. M. Taylor, S. G. Young, and B. J. McCarthy. 1991. Expression of carboxyl-terminally truncated forms of human apolipoprotein B in rat hepatoma cells. J. Biol. Chem. 266: 3300-3308.
24. Schumaker, V. N., M. L. Phillips, and J. E. Chatterton. 1994. Apolipoprotein B and low-density lipoprotein structure: implications for biosynthesis of triglyceride-rich lipoproteins. Adv. Protein Chem. 45: 205-248.
25. Graham, D., K. Lesley, J. J. Timothy, C. P. Tina, J. Richard, C. R. Pullinger, and J. Scott. 1991. Carboxyl-terminal truncation of apolipoprotein B results in gradual loss of the ability to form buoyant lipoproteins in cultured human and rat liver cell lines. Biochemistry. 30: 5616-5621.
26. Herscovitz, H., M. Hadzopoulou-Cladaras, M. T. Walsh, C. Cladaras, V. I. Zannis, and D. M. Small. 1991. Expression, secretion and lipid-binding characterization of the N-terminal 17% of the apolipoprotein B. Proc. Natl. Acad. Sci. USA 88: 7313-7317.