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PDBsum entry 4i4x
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Sugar binding protein
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PDB id
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4i4x
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PDB id:
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| Name: |
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Sugar binding protein
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Title:
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Bel beta-trefoil complex with t-antigen disaccharide
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Structure:
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Bel beta-trefoil. Chain: a, b, c, d
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Source:
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Boletus edulis. King bolete mushroom. Organism_taxid: 36056
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Resolution:
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1.72Å
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R-factor:
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0.178
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R-free:
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0.205
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Authors:
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M.Bovi,L.Cenci,M.Perduca,S.Capaldi,M.E.Carrizo,L.Civiero, L.R.Chiarelli,M.Galliano,H.L.Monaco
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Key ref:
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M.Bovi
et al.
(2013).
BEL β-trefoil: a novel lectin with antineoplastic properties in king bolete (Boletus edulis) mushrooms.
Glycobiology,
23,
578-592.
PubMed id:
DOI:
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Date:
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28-Nov-12
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Release date:
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24-Apr-13
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PROCHECK
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Headers
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References
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R4GRU9
(R4GRU9_BOLED) -
BEL beta-trefoil from Boletus edulis
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Seq:
Struc:
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146 a.a.
146 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Glycobiology
23:578-592
(2013)
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PubMed id:
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BEL β-trefoil: a novel lectin with antineoplastic properties in king bolete (Boletus edulis) mushrooms.
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M.Bovi,
L.Cenci,
M.Perduca,
S.Capaldi,
M.E.Carrizo,
L.Civiero,
L.R.Chiarelli,
M.Galliano,
H.L.Monaco.
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ABSTRACT
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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.
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