Abstract
THE binding of lipids into globules by the serum lipid-binding proteins depends on the unique structures of these proteins. Many have a high α helix content1–4 which is enhanced by the binding of lipid, and their amino acid sequences5–8 suggest that the helices are often ‘amphipathic’ with a long hydrophobic face buried in the lipid surface9,10 and an exposed polar face which interacts specifically with the charged head groups of phospholipids such as lecithin. Apolipoprotein-A-I (or -Gln-I) is the larger of the two major human high density plasma lipoproteins11–13, with 245 amino acids and a helix content3 of about 70% in the native complex. Physical measurements10,14–16 and a study of the sequence10,11 suggest that in several of its complexes reconstituted from phospholipids, the protein has a loosely folded structure of between 9 and 13 helices which float in the surface of a disk-shaped bilayer 5.5 nm thick and 11 nm in diameter17,18, rather as logs float on water. With pure lecithin and A-I protein, each complex contains two protein and about 200 lipid molecules19. The pattern of non-polar groups in A-I protein is unusually regular, even for a helical structure, and this suggested that the sequence may have evolved by internal gene duplication20 in the same way as some other long repetitive structures21,22. Barker and Dayhorf23, Fitch24 and I independently found a regular 11- or 22-residue repeat pattern in it. Here I report an analysis of the repeats and discuss their structural significance.
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References
Morrisett, J. D., David, J. S. K., Pownall, H. J. & Gotto, A. M. Biochemistry 12, 1290–1299 (1973).
Jackson, R. L., Morrisett, J. D., Pownall, H. J. & Gotto, A. M. J. biol. Chem. 248, 5218–5224 (1973).
Lux, S. E., Hirz, R., Shrager, R. I. & Gotto, A. M. J. biol. Chem. 247, 2598–2606 (1972).
Jackson, R. L. et al. J. biol. Chem. 249, 5314–5320 (1974).
Baker, H. N., Gotto, A. M. & Jackson, R. L. J. biol. Chem. 250, 2725–2738 (1975).
Jackson, R. L. et al. J. biol. Chem. 249, 5308–5313 (1974).
Brewer, H. B., Lux, S. E., Ronan, R. & John, K. M. Proc. natn. Acad. Sci. U.S.A. 69, 1304–1308 (1972).
Brewer, H. B., Shulman, R., Herbert, P., Ronan, R. & Wehrly, K. Adv. exp. Med. Biol. 26, 280 (1972).
Segrest, J. P., Jackson, R. L., Morrisett, J. D. & Gotto, A. M. FEBS Lett. 38, 247–253 (1974).
Atkinson, D., Smith, H. M., Dickson, J. & Austin, J. P. Eur. J. Biochem. 64, 541–547 (1976).
Baker, H. N., Delahunty, T., Gotto, A. M. & Jackson, R. L. Proc. natn. Acad. Sci. U.S.A. 71, 3631–3634 (1974).
Scanu, A. M., Edelstein, C. & Keim, P. in The Plasma Proteins, second edit. I (ed. F. W. Putnam) 318–391 (Academic, New York, 1975).
Morrisett, J. D., Jackson, R. L. & Gotto, A. M. A. Rev. Biochem. 44, 183–207 (1975).
Finer, E. G., Henry, R., Leslie, R. B. & Robertson, R. N. Biochem. Biophys. Acta 380, 320–337 (1975).
Forte, T. M., Nichols, A. V., Gong, E. L., Lux, S. E. & Levy, R. I. Biochem. biophys. Acta. 248, 381–386 (1971).
Scanu, A. M. Biochem. biophys. Acta 265, 471–508 (1972).
Muller, K., Laggner, P., Kratky, O., Kostner, G., Holasek, A. & Glatter, O. FEBS Lett. 40, 213–218 (1974).
Andrews, A. L. et al. Eur. J. Biochem. 64, 549–563 (1976).
Hauser, H., Henry, R., Leslie, R. B. & Stubbs, J. M. Eur. J. Biochem. 48, 583–594 (1974).
Ohno, S. Evolution by Gene Duplication (London, Allen and Unwin, London, 1970).
McLachlan, A. D., Stewart, M. & Smillie, L. B. J. molec. Biol. 98, 281–291 (1975).
Brown, J. R. Fedn Proc. 35, 2141–2144 (1976).
Barker, W. C. & Dayhoff, M. O. in Atlas of Protein Sequence and Structure 5, suppl. 2, 253–254 (National Biomedical Research Foundation, Washington DC, 1976).
Fitch, W. M. in Proceedings of La Table Ronde on Biomolecular Evolution (ed. J. Mathieu) (Roussel, Uclaf, Paris, in the press).
McLachlan, A. D. J. molec. Biol. 61, 409–421 (1971).
McLachlan, A. D. J. molec. Biol. 107, 159–174 (1976).
Perutz, M. F., Kendrew, J. C. & Watson, H. C. J. molec. Biol. 13, 669–678 (1965).
Tall, A. R., Shipley, G. G. & Small, D. M. J. biol. Chem. 251, 3749–3755 (1976).
Henderson, R. & Unwin, P. N. T. Nature 257, 28–32 (1975).
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MCLACHLAN, A. Repeated helical pattern in apolipoprotein-A-I. Nature 267, 465–466 (1977). https://doi.org/10.1038/267465a0
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DOI: https://doi.org/10.1038/267465a0
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