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Computer modelling approach to study the modes of binding of alpha- and beta-anomers of D-galactose, D-fucose and D-glucose to L-arabinose-binding protein

Mukhopadhyay, Chaitali and Rao, VSR (1989) Computer modelling approach to study the modes of binding of alpha- and beta-anomers of D-galactose, D-fucose and D-glucose to L-arabinose-binding protein. In: International Journal of Biological Macromolecules, 11 (4). pp. 194-200.

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Official URL: http://dx.doi.org/10.1016/0141-8130(89)90068-8

Abstract

The modes of binding of alpha- and beta-anomers of D-galactose, D-fucose and D-glucose to L-arabinose-binding protein (ABP) have been studied by energy minimization using the low resolution (2.4 A) X-ray data of the protein. These studies suggest that these sugars preferentially bind in the alpha-form to ABP, unlike L-arabinose where both alpha- and beta-anomers bind almost equally. The best modes of binding of alpha- and beta-anomers of D-galactose and D-fucose differ slightly in the nature of the possible hydrogen bonds with the protein. The residues Arg 151 and Asn 232 of ABP from bidentate hydrogen bonds with both L-arabinose and D-galactose, but not with D-fucose or D-glucose. However in the case of L-arabinose, Arg 151 forms hydrogen bonds with the hydroxyl group at the C-4 atom and the ring oxygen, whereas in case of D-galactose it forms bonds with the hydroxyl groups at the C-4 and C-6 atoms of the pyranose ring. The calculated conformational energies also predict that D-galactose is a better inhibitor than D-fucose and D-glucose, in agreement with kinetic studies. The weak inhibitor D-glucose binds preferentially to one domain of ABP leading to the formation of a weaker complex. Thus these studies provide information about the most probable binding modes of these sugars and also provide a theoretical explanation for the observed differences in their binding affinities.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Elsevier Science.
Keywords: l-arabinose-binding protein;protein—carbohydrate interaction; molecular fit;energy minimization.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 09 Aug 2010 06:04
Last Modified: 19 Sep 2010 06:13
URI: http://eprints.iisc.ernet.in/id/eprint/31192

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