3QDT

Structure of Boletus edulis lectin in complex with T-antigen disaccharide

Summary for 3QDT

• Entry DOI: 10.2210/pdb3qdt/pdb
• Related: 3QDS 3QDT 3QDV 3QDW 3QDX 3QDY
• Related PRD ID: PRD_900084
• Descriptor: BOLETUS EDULIS LECTIN, beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-alpha-D-galactopyranose (3 entities in total)
• Functional Keywords: boletus edulis, lectin, mushroom, t-antigen, carbohydrate, sugar binding protein
• Biological source: Boletus edulis
• Total number of polymer chains: 2
• Total formula weight: 32470.37

Authors

Bovi, M.,Carrizo, M.E.,Capaldi, S.,Perduca, M.,Chiarelli, L.R.,Galliano, M.,Monaco, H.L. (deposition date: 2011-01-19, release date: 2011-02-23, Last modification date: 2024-10-30)

Primary citation

Bovi, M.,Carrizo, M.E.,Capaldi, S.,Perduca, M.,Chiarelli, L.R.,Galliano, M.,Monaco, H.L.
Structure of a lectin with antitumoral properties in king bolete (Boletus edulis) mushrooms.
Glycobiology, 21:1000-1009, 2011

PubMed Abstract: A 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 (B. edulis lectin). BEL inhibits selectively the proliferation of several malignant cell lines and binds the neoplastic cell-specific T-antigen disaccharide, Galβ1-3GalNAc. 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 Å 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.

PubMed: 21303815
DOI: 10.1093/glycob/cwr012

Experimental method

X-RAY DIFFRACTION (1.3 Å)