Pantoja-Uceda D, Bruix M, Santoro J, Rico M, Monsalve R, Villalba M
Instituto de Química Física Rocasolano, CSIC, Serrano 119, Madrid 28006, Spain.
Biochem Soc Trans. 2002 Nov;30(Pt 6):919-24. doi: 10.1042/bst0300919.
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 alpha-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.
本文描述了三种不同的2S白蛋白种子蛋白在不同精细程度下的核磁共振溶液结构，即来自油菜籽的重组前napin蛋白前体、来自蓖麻的重组RicC3以及来自向日葵（Helianthus annuus）的富含蛋氨酸的蛋白。所得的共同结构由一束五个α螺旋组成，折叠成右手超螺旋。该结构与其他植物蛋白非常相似：大豆的疏水蛋白、非特异性脂质转运蛋白和淀粉酶/胰蛋白酶抑制剂。讨论了这些家族结构的异同，以及它们与致敏性可能的关系。
