Sekharudu, Y.Chandra and Rao, VSR (1985) Theoretical-Studies on the Modes of Binding of Some of the Beta-Glycosidically Linked Glucobioses to Concanavalin-A. In: International Journal of Biological Macromolecules, 7 (6). pp. 349-356.
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Abstract
The probable modes of binding for methyl-α-d-sophoroside, methyl-β-d-sophoroside, laminariboise and cellobiose to concanavalin A have been determined using theoretical methods. Methyl-d-sophorosides can bind to concanavalin A in two modes, i.e. by placing their reducing as well as non-reducing sugar units in the carbohydrate specific binding site, whereas laminaribiose and cellobiose can reach the binding site only with their non-reducing glucose units. However, the probability for methyl-α-d-sophoroside to bind to concanavalin A with its reducing sugar residue as the occupant of the binding site is much higher than it is with its non-reducing sugar residue as the occupant of the sugar binding site. A few of the probable conformers of methyl-β-d-sophoroside can bind to concanavalin A with either the reducing or non-reducing glucose unit. Higher energy conformers of cellobiose or laminaribiose can reach the binding site with their non-reducing residues alone. The relative differences in the binding affinities of these disaccharides are mainly due to the differences in the availability of proper conformers which can reach the binding site and to non-covalent interactions between the sugar and the protein. This study also suggests that though the sugar binding site of concanavalin A accommodates a single sugar residue, the residue outwards from the binding site also interacts with concanavalin A, indicating the existence of extended concanavalin A carbohydrate interactions.
Item Type: | Journal Article |
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Publication: | International Journal of Biological Macromolecules |
Publisher: | Elsevier Science |
Additional Information: | The copyright of this article belongs to Elsevier Science |
Keywords: | Concanavalin A; glucobioses; protein-carbohydrate interaction; computer modelling studies |
Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit |
Date Deposited: | 09 Nov 2009 13:17 |
Last Modified: | 19 Sep 2010 05:31 |
URI: | http://eprints.iisc.ac.in/id/eprint/20126 |
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