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PDBsum entry 6vc3
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Sugar binding protein
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PDB id
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6vc3
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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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Peanut lectin complexed with s-beta-d-thiogalactopyranosyl 6-deoxy-6- s-propynyl-beta-d-glucopyranoside (stg)
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Structure:
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Galactose-binding lectin. Chain: a, b, c, d. Synonym: agglutinin,pna
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Source:
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Arachis hypogaea. Peanut. Organism_taxid: 3818
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Resolution:
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1.95Å
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R-factor:
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0.268
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R-free:
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0.283
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Authors:
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L.H.Otero,E.D.Primo,A.J.Cagnoni,M.E.Cano,S.Klinke,F.A.Goldbaum, M.L.Uhrig
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Key ref:
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A.J.Cagnoni
et al.
(2020).
Crystal structures of peanut lectin in the presence of synthetic β-N- and β-S-galactosides disclose evidence for the recognition of different glycomimetic ligands.
Acta Crystallogr D Struct Biol,
76,
1080-1091.
PubMed id:
DOI:
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Date:
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20-Dec-19
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Release date:
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28-Oct-20
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PROCHECK
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Headers
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References
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P02872
(LECG_ARAHY) -
Galactose-binding lectin from Arachis hypogaea
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Seq:
Struc:
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273 a.a.
232 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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DOI no:
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Acta Crystallogr D Struct Biol
76:1080-1091
(2020)
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PubMed id:
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Crystal structures of peanut lectin in the presence of synthetic β-N- and β-S-galactosides disclose evidence for the recognition of different glycomimetic ligands.
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A.J.Cagnoni,
E.D.Primo,
S.Klinke,
M.E.Cano,
W.Giordano,
K.V.Mariño,
J.Kovensky,
F.A.Goldbaum,
M.L.Uhrig,
L.H.Otero.
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ABSTRACT
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Carbohydrate-lectin interactions are involved in important cellular recognition
processes, including viral and bacterial infections, inflammation and tumor
metastasis. Hence, structural studies of lectin-synthetic glycan complexes are
essential for understanding lectin-recognition processes and for the further
design of promising chemotherapeutics that interfere with sugar-lectin
interactions. Plant lectins are excellent models for the study of the
molecular-recognition process. Among them, peanut lectin (PNA) is highly
relevant in the field of glycobiology because of its specificity for
β-galactosides, showing high affinity towards the Thomsen-Friedenreich antigen,
a well known tumor-associated carbohydrate antigen. Given this specificity, PNA
is one of the most frequently used molecular probes for the recognition of tumor
cell-surface O-glycans. Thus, it has been extensively used in glycobiology for
inhibition studies with a variety of β-galactoside and β-lactoside ligands.
Here, crystal structures of PNA are reported in complex with six novel synthetic
hydrolytically stable β-N- and β-S-galactosides. These complexes disclosed key
molecular-binding interactions of the different sugars with PNA at the atomic
level, revealing the roles of specific water molecules in protein-ligand
recognition. Furthermore, binding-affinity studies by isothermal titration
calorimetry showed dissociation-constant values in the micromolar range, as well
as a positive multivalency effect in terms of affinity in the case of the
divalent compounds. Taken together, this work provides a qualitative structural
rationale for the upcoming synthesis of optimized glycoclusters designed for the
study of lectin-mediated biological processes. The understanding of the
recognition of β-N- and β-S-galactosides by PNA represents a benchmark in
protein-carbohydrate interactions since they are novel synthetic ligands that do
not belong to the family of O-linked glycosides.
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