A novel mode of carbohydrate recognition in jacalin, a Moraceae plant lectin with a β-prism fold
R Sankaranarayanan, K Sekar, R Banerjee… - Nature structural …, 1996 - nature.com
Nature structural biology, 1996•nature.com
Jacalin, a tetrameric two-chain lectin (66,000 M r) from jackfruit seeds, is highly specific for
the tumour associated T-antigenic disaccharide. The crystal structure of jacalin with methyl-α-
D-galactose reveals that each subunit has a three-fold symmetric β-prism fold made up of
three four-stranded β-sheets. The lectin exhibits a novel carbohydrate-binding site involving
the N terminus of the α-chain which is generated through a post-translational modification
involving proteolysis, the first known instance where such a modification has been used to …
the tumour associated T-antigenic disaccharide. The crystal structure of jacalin with methyl-α-
D-galactose reveals that each subunit has a three-fold symmetric β-prism fold made up of
three four-stranded β-sheets. The lectin exhibits a novel carbohydrate-binding site involving
the N terminus of the α-chain which is generated through a post-translational modification
involving proteolysis, the first known instance where such a modification has been used to …
Abstract
Jacalin, a tetrameric two-chain lectin (66,000 Mr) from jackfruit seeds, is highly specific for the tumour associated T-antigenic disaccharide. The crystal structure of jacalin with methyl-α-D-galactose reveals that each subunit has a three-fold symmetric β-prism fold made up of three four-stranded β-sheets. The lectin exhibits a novel carbohydrate-binding site involving the N terminus of the α-chain which is generated through a post-translational modification involving proteolysis, the first known instance where such a modification has been used to confer carbohydrate specificity. This new lectin fold may be characteristic of the Moraceae plant family. The structure provides an explanation for the relative affinities of the lectin for galactose derivatives and provides insights into the structural basis of its T-antigen specificity.
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