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4I4R

BEL beta-trefoil apo crystal form 4

4I4R の概要
エントリーDOI10.2210/pdb4i4r/pdb
関連するPDBエントリー4I4O 4I4P 4I4Q 4I4S 4I4U 4I4V 4I4X 4I4Y
分子名称BEL-beta trefoil, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL (3 entities in total)
機能のキーワードlectin, fruiting bodies, sugar binding protein
由来する生物種Boletus edulis (king bolete mushroom)
タンパク質・核酸の鎖数4
化学式量合計67618.42
構造登録者
Bovi, M.,Cenci, L.,Perduca, M.,Capaldi, S.,Carrizo, M.E.,Civiero, L.,Chiarelli, L.R.,Galliano, M.,Monaco, H.L. (登録日: 2012-11-28, 公開日: 2013-04-24, 最終更新日: 2023-09-20)
主引用文献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: 23213111
DOI: 10.1093/glycob/cws164
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.77 Å)
構造検証レポート
Validation report summary of 4i4r
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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