Structural Basis of Functional Mimicry between Carbohydrate and Peptide Ligands of Con A

Crystallographic studies have shown independent binding sites for sugar and peptide ligands of concanavalin A, although they were considered functional mimics based on biochemical experiments. The topological correlation of 12-residue peptide with different carbohydrate ligands of concanavalin A sho...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2000-06, Vol.272 (3), p.843-849
Main Authors: Jain, Deepti, Kaur, Kanwal J., Goel, Manisha, Salunke, Dinakar M.
Format: Article
Language:English
Subjects:
Amino Acid Motifs
Amino Acid Sequence
Binding Sites
Carbohydrate Metabolism
carbohydrate-mimicking peptide
Carbohydrates - chemistry
Concanavalin A - chemistry
Concanavalin A - metabolism
Glycoproteins - chemistry
Glycoproteins - metabolism
Ligands
Mannose - metabolism
Methylmannosides - metabolism
Models, Molecular
Molecular Conformation
molecular docking
Molecular Mimicry
molecular recognition
Peptides - chemistry
Peptides - metabolism
Protein Binding
receptor-binding site
Static Electricity
Structure-Activity Relationship
Substrate Specificity
Surface Properties
Thermodynamics
Trioses - chemistry
Trioses - metabolism
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Summary:Crystallographic studies have shown independent binding sites for sugar and peptide ligands of concanavalin A, although they were considered functional mimics based on biochemical experiments. The topological correlation of 12-residue peptide with different carbohydrate ligands of concanavalin A showed similarity between trimannose and the YPY region of the peptide establishing structural mimicry. Molecular docking of trimannose and the YPY motif on the reciprocal binding sites revealed equivalent interactions and energetics implying that the peptide-binding sites may constitute additional sugar-binding subsites of concanavalin A. The binding of a mannose-rich neoglycoprotein with significantly higher affinity compared with that of the methyl α-d-mannopyranoside is consistent with this interpretation.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.2000.2871