Solution structure of allergenic 2 S albumins. (November 2002)

• Record Type: Journal Article
• Authors: Pantoja-Uceda, D.; Bruix, M.; Santoro, J.; Rico, M.; Monsalve, R.; Villalba, M.
• Is Part Of: Biochemical Society transactions. Volume 30:Number 6(2002)
• Page Start: 919
• Page End: 924
• Publication Date: 2002-11
• Subjects: Brassica napus -- Helianthus annuus -- NMR -- Ricinus communis -- seed proteins; HPS, hydrophobic protein from soybean -- HSQC, heteronuclear single-quantum coherence -- LTP, lipid transfer protein -- nsLTP, non-specific lipid transfer protein -- NOE, nuclear Overhauser effect -- SFA-8, methionine-rich 2 S albumin 8 from sunflower; Biochemistry -- Congresses; 572
• DOI: 10.1042/bst0300919
• Languages: English
• ISSNs: 0300-5127

Abstract

Abstract : 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.