Solution structure of allergenic 2 S albumins.
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.
Pantoja-Uceda
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D
Instituto de Química Física Rocasolano, CSIC, Serrano 119, Madrid 28006, Spain.
Bruix
M
M
Santoro
J
J
Rico
M
M
Monsalve
R
R
Villalba
M
M
D055516:2S Albumins, Plant; D000485:Allergens / Q000737:chemistry*; D000595:Amino Acid Sequence; D052179:Antigens, Plant; D029688:Brassica napus / Q000378:metabolism; D018076:DNA, Complementary / Q000378:metabolism; D006368:Helianthus / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry*; D010944:Plants / Q000378:metabolism; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D017386:Sequence Homology, Amino Acid
D055516:2S Albumins, Plant; C541551:2S storage protein, Ricinus communis; D000485:Allergens; D052179:Antigens, Plant; D018076:DNA, Complementary; D010940:Plant Proteins; D011994:Recombinant Proteins; C067568:methionine-rich 2S protein, Helianthus; C050363:napin protein, Brassica napus