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5U3E

Crystal Structure of Native Lectin from Canavalia bonariensis Seeds (CaBo) complexed with alpha-methyl-D-mannoside

Summary for 5U3E
Entry DOI10.2210/pdb5u3e/pdb
DescriptorCanavalia bonariensis seed lectin, methyl alpha-D-mannopyranoside, MANGANESE (II) ION, ... (5 entities in total)
Functional Keywordscanavalia bonariensis, lectin, alpha-methyl-d-mannoside., sugar binding protein
Biological sourceCanavalia bonariensis
Total number of polymer chains1
Total formula weight25840.40
Authors
Primary citationCavada, B.S.,Silva, M.T.L.,Osterne, V.J.S.,Pinto-Junior, V.R.,Nascimento, A.P.M.,Wolin, I.A.V.,Heinrich, I.A.,Nobre, C.A.S.,Moreira, C.G.,Lossio, C.F.,Rocha, C.R.C.,Martins, J.L.,Nascimento, K.S.,Leal, R.B.
Canavalia bonariensis lectin: Molecular bases of glycoconjugates interaction and antiglioma potential.
Int. J. Biol. Macromol., 106:369-378, 2018
Cited by
PubMed Abstract: 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.
PubMed: 28803976
DOI: 10.1016/j.ijbiomac.2017.08.023
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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