The NMR solution structures at different levels of refinement of three different 2 S albumin seed proteins, the recombinant pronapin precursor from Brassica napus, the recombinant RicC3 from Ricinus communis and the methionine-rich protein from sunflower (Helianthus annuus), are described. The resulting common structure consists of a bundle of five α-helices, folded in a right-handed superhelix. The structure is very similar to that of other plant proteins: the hydrophobic protein from soybean, non-specific lipid transfer proteins and amylase/trypsin inhibitors. Analogies and differences in the structures of these families, as well as their possible relationship to allergenicity, are discussed.
Conference Article| November 01 2002
Solution structure of allergenic 2 S albumins
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D. Pantoja-Uceda, M. Bruix, J. Santoro, M. Rico, R. Monsalve, M. Villalba; Solution structure of allergenic 2 S albumins. Biochem Soc Trans 1 November 2002; 30 (6): 919–924. doi: https://doi.org/10.1042/bst0300919
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