Computer modelling studies on the modes of binding of some of the α- glycosidically linked disaccharides to concanavalin A.
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Date
1985-08
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Abstract
The possible modes of binding of kojibiose, nigerose, maltose and ManPα(1
→2)Man to concanavalin A have been investigated using computer modelling studies. While
α12 linked disaccharides bind to concanavalin A in two modes, i.e. by placing the reducing as
well as non-reducing sugar units in the sugar binding site, nigerose or maltose can bind only in
one mode, i.e. by placing the non-reducing sugar unit in the binding site. Though, both the
sugar residues in α 12 linked disaccharides can reach the binding site, the preference is high for
the non-reducing unit. When the non-reducing residue, in any of these disaccharides, enters the
binding site, the allowed orientations and the possible hydrogen bonds with the protein seem
to be independent of the glycosidic linkage. However, the number of hydrogen bonds the
outward sugar residue forms with the protein are dependent on the type of linkage. Atleast one
of the hydroxyl groups adjacent to the glycosidic linkage on the outward sugar residue is
involved in the formation of a hydrogen bond with the protein suggesting the presence of an
extended binding site. The orientation of the reducing sugar residue in the extended binding
site is dependent on the linkage. Its orientation in nigerose is flipped when compared to that
found in kojibiose or maltose leading to different non-covalent interactions with the protein
which affect their binding affinities.
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Keywords
Concanavalin A, modes of binding of disaccharides to, computer modelling studies, protein-carbohydrate interactions
Citation
Sekharudu Y Chandra, Rao V S R. Computer modelling studies on the modes of binding of some of the α- glycosidically linked disaccharides to concanavalin A. Journal of Biosciences. 1985 Aug; 8(1&2): 389-401.