4I4V
BEL beta-trefoil complex with N-acetylgalactosamine
Summary for 4I4V
| Entry DOI | 10.2210/pdb4i4v/pdb |
| Related | 4I4O 4I4P 4I4Q 4I4R 4I4S 4I4U 4I4X 4I4Y |
| Descriptor | BEL beta-trefoil, 2-acetamido-2-deoxy-beta-D-galactopyranose, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total) |
| Functional Keywords | lectin, fruiting bodies, sugar binding protein |
| Biological source | Boletus edulis (king bolete mushroom) |
| Total number of polymer chains | 4 |
| Total formula weight | 68579.24 |
| Authors | Bovi, M.,Cenci, L.,Perduca, M.,Capaldi, S.,Carrizo, M.E.,Civiero, L.,Chiarelli, L.R.,Galliano, M.,Monaco, H.L. (deposition date: 2012-11-28, release date: 2013-04-24, Last modification date: 2023-09-20) |
| Primary citation | Bovi, M.,Cenci, L.,Perduca, M.,Capaldi, S.,Carrizo, M.E.,Civiero, L.,Chiarelli, L.R.,Galliano, M.,Monaco, H.L. BEL {beta}-trefoil: A novel lectin with antineoplastic properties in king bolete (Boletus edulis) mushrooms. Glycobiology, 23:578-592, 2013 Cited by PubMed Abstract: A novel lectin was purified from the fruiting bodies of king bolete mushrooms (Boletus edulis, also called porcino, cep or penny bun). The lectin was structurally characterized i.e its amino acid sequence and three-dimensional structure were determined. The new protein is a homodimer and each protomer folds as β-trefoil domain and therefore we propose the name Boletus edulis lectin (BEL) β-trefoil to distinguish it from the other lectin that has been described in these mushrooms. The lectin has potent anti-proliferative effects on human cancer cells, which confers to it an interesting therapeutic potential as an antineoplastic agent. Several crystal forms of the apoprotein and of complexes with different carbohydrates were studied by X-ray diffraction. The structure of the apoprotein was solved at 1.12 Å resolution. The interaction of the lectin with lactose, galactose, N-acetylgalactosamine and T-antigen disaccharide, Galβ1-3GalNAc, was examined in detail. All the three potential binding sites present in the β-trefoil fold are occupied in at least one crystal form and are described in detail in this paper. No important conformational changes are observed in the lectin when comparing its co-crystals with carbohydrates with those of the ligand-free protein. PubMed: 23213111DOI: 10.1093/glycob/cws164 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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