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PDBsum entry 5u3e
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Sugar binding protein
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PDB id
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5u3e
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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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Crystal structure of native lectin from canavalia bonariensis seeds (cabo) complexed with alpha-methyl-d-mannoside
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Structure:
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Canavalia bonariensis seed lectin. Chain: a
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Source:
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Canavalia bonariensis. Organism_taxid: 192414
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Resolution:
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2.30Å
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R-factor:
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0.231
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R-free:
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0.283
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Authors:
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M.T.L.Silva,V.J.S.Osterne,V.R.Pinto-Junior,M.Q.Santiago,D.A.Araripe, A.H.B.Neco,J.C.Silva-Filho,J.L.Martins,C.R.C.Rocha,R.B.Leal, K.S.Nascimento,B.S.Cavada
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Key ref:
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B.S.Cavada
et al.
(2018).
Canavalia bonariensis lectin: Molecular bases of glycoconjugates interaction and antiglioma potential.
Int J Biol Macromol,
106,
369-378.
PubMed id:
DOI:
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Date:
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02-Dec-16
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Release date:
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23-Aug-17
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PROCHECK
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Headers
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References
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P58906
(LECA_CANBN) -
Lectin CaBo (Fragment) from Canavalia bonariensis
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Seq:
Struc:
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281 a.a.
235 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 26 residue positions (black
crosses)
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DOI no:
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Int J Biol Macromol
106:369-378
(2018)
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PubMed id:
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Canavalia bonariensis lectin: Molecular bases of glycoconjugates interaction and antiglioma potential.
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B.S.Cavada,
M.T.L.Silva,
V.J.S.Osterne,
V.R.Pinto-Junior,
A.P.M.Nascimento,
I.A.V.Wolin,
I.A.Heinrich,
C.A.S.Nobre,
C.G.Moreira,
C.F.Lossio,
C.R.C.Rocha,
J.L.Martins,
K.S.Nascimento,
R.B.Leal.
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ABSTRACT
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CaBo is a mannose/glucose-specific lectin purified from seeds of Canavalia
bonariensis. In the present work, we report the CaBo crystal structure
determined to atomic resolution in the presence of X-man, a specific ligand.
Similar to the structural characteristics of other legume lectins, CaBo
presented the jellyroll motif, a metal binding site occupied by calcium and
manganese ions close to the carbohydrate-recognition domain (CRD). In vitro test
of CaBo cytotoxicity against glioma cells demonstrated its ability to decrease
the cellular viability and migration by induction of autophagy and cell death.
Molecular docking simulations corroborate previous data indicating that the
lectin's biological activities occur mostly through interactions with
glycoproteins since the lectin interacted favorably with several N-glycans,
especially those of the high-mannose type. Together, these results suggest that
CaBo interacts with glycosylated cell targets and elicits a remarkable
antiglioma activity.
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