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- W2014310320 abstract "The modes of binding of α- and β-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 Å) X-ray data of the protein. These studies suggest that these sugars preferentially bind in the α-form to ABP, unlike l-arabinose where both α- and β-anomers bind almost equally. The best modes of binding of α- and β-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." @default.
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- W2014310320 date "1989-08-01" @default.
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- W2014310320 title "Computer modelling approach to study the modes of binding of α- and β-anomers of d-galactose, d-fucose and d-glucose to l-arabinose-binding protein" @default.
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- W2014310320 doi "https://doi.org/10.1016/0141-8130(89)90068-8" @default.
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