Abstract
LTPs transfer phospholipids between membranes “in vitro” (1). Plant LTPs are still in search of an “in vivo” role. These proteins share in common structural and functional properties (1). NMR and X-ray crystallography have been carried out on plant LTPs. These proteins comprise a single compact domain with four alpha-helices and a long C-terminal region. They have a tunnel-like hydrophobic cavity able to accomodate fatty acids (2–3). A complex between maize LTP and palmitic acid has been indeed recently crystallized (2). This recent model of ns-LTPs gives a basis for understanding the function of LTPs in relation to the transfer and binding of molecules containing acyl chains (PLP, fatty acids, acyl-CoA).
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- ELISA:
-
enzyme link immunosorbent assay
- ns-LTP:
-
non specific Lipid Transfer Protein
- PC:
-
phosphatidylcholine
- PLP:
-
phospholipid.
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© 1997 Springer Science+Business Media Dordrecht
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Guerbette, F., Jolliot, A., Kader, JC., Grosbois, M. (1997). Binding of Lipids on Lipid Transfer Proteins. In: Williams, J.P., Khan, M.U., Lem, N.W. (eds) Physiology, Biochemistry and Molecular Biology of Plant Lipids. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-2662-7_41
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DOI: https://doi.org/10.1007/978-94-017-2662-7_41
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