Structural highlights
Publication Abstract from PubMedA novel lectin has been isolated from the fruiting bodies of the common edible mushroom Boletus edulis (king bolete, penny bun, porcino, or cep) by affinity chromatography on a chitin column. We propose for the lectin the name BEL (Boletus edulis lectin). BEL inhibits selectively the proliferation of several malignant cell lines and binds the neoplastic cell specific T-antigen disaccharide, Galbeta1-3GalNAc. The lectin was structurally characterized: the molecule is a homotetramer and the 142 amino acid sequence of the chains was determined. The protein belongs to the saline-soluble family of mushroom fruiting body specific lectins. BEL was also crystallized and its three-dimensional structure was determined by X-ray diffraction to 1.15 A resolution. The structure is similar to that of Agaricus bisporus lectin. Using the appropriate co-crystals, the interactions of BEL with specific mono and disaccharides were also studied by X-ray diffraction. The six structures of carbohydrate complexes reported here provide details of the interactions of the ligands with the lectin and shed light on the selectivity of the two distinct binding sites present in each protomer. STRUCTURE OF A LECTIN WITH ANTITUMORAL PROPERTIES IN KING BOLETE (Boletus edulis) MUSHROOMS.,Bovi M, Carrizo ME, Capaldi S, Perduca M, Chiarelli LR, Galliano M, Monaco HL Glycobiology. 2011 Feb 8. PMID:21303815[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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