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Assignment of 1H and 15N resonances and secondary structure of the recombinant RicC3 of 2S albumin storage protein from Ricinus communis [5]

AuthorsPantoja-Uceda, D.; Bruix, M. CSIC ORCID; Varela, Javier CSIC ; López-Lucendo, María F. CSIC; Giménez-Gallego, Guillermo CSIC; Rico, Manuel CSIC; Santoro, Jorge CSIC
KeywordsNMR assignments
Ricinus communis
2S Albumin
Secondary structure
Issue DateAug-2002
PublisherSpringer Nature
CitationJournal of Biomolecular NMR 23: 331-332 (2002)
AbstractThe 2S albumins are storage proteins widely distributed in plant seeds. They are small proteins (12 to 15 kDa) generally composed of two different polypeptide chains linked by disulphide bridges. Due to their amino acid compositions, their high content in the protein bodies of the seeds, and their mobilization during germination, a role as nitrogen and sulfur donor has been proposed for these proteins (Youle and Huang, 1978). However, other activities have been ascribed to the 2S albumins: they have been shown to act as antifungal, serine protease inhibitors, and calmodulin antagonists. Moreover, in recent years, several 2S albumins have been described as allergens, suggesting that this family of proteins is intrinsically allergenic. In addition to their biochemical interest, the 2S albumins have been used, by means of genetic engineering as carriers for the synthesis of biologically active peptides (Vandekerckhove et al., 1989), as well as to improve the nutritional properties of grain crops by increasing their content of essential amino acids. One of the products of the Ricinus communis 2S seed storage protein, termed RicC3 (Bashir et al., 1998) constitutes the peptidic component of the immunomodulator Inmunoferon, a widely used pharmaceutical speciality (Varela et al., 2002).
Publisher version (URL)
Identifiersdoi: 10.1023/A:1020231706895
issn: 0925-2738
e-issn: 1573-5001
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(IQFR) Artículos

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