1kuj | pdb_00001kuj
Crystal structure of Jacalin complexed with 1-O-methyl-alpha-D-mannose
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Overview
Evidence is presented that the specificity of jacalin, the seed lectin from jack fruit (Artocarpus integrifolia), is not directed exclusively against the T-antigen disaccharide Galbeta1,3GalNAc, lactose and galactose, but also against mannose and oligomannosides. Biochemical analyses based on surface-plasmon-resonance measurements, combined with the X-ray-crystallographic determination of the structure of a jacalin-alpha-methyl-mannose complex at 2 A resolution, demonstrated clearly that jacalin is fully capable of binding mannose. Besides mannose, jacalin also interacts readily with glucose, N-acetylneuraminic acid and N-acetylmuramic acid. Structural analyses demonstrated that the relatively large size of the carbohydrate-binding site enables jacalin to accommodate monosaccharides with different hydroxyl conformations and provided unambiguous evidence that the beta-prism structure of jacalin is a sufficiently flexible structural scaffold to confer different carbohydrate-binding specificities to a single lectin.
About this Structure
1KUJ is a Protein complex structure of sequences from Artocarpus integer with MMA as ligand. Full crystallographic information is available from OCA.
Reference
Structural basis for the unusual carbohydrate-binding specificity of jacalin towards galactose and mannose., Bourne Y, Astoul CH, Zamboni V, Peumans WJ, Menu-Bouaouiche L, Van Damme EJ, Barre A, Rouge P, Biochem J. 2002 May 15;364(Pt 1):173-80. PMID:11988090
Page seeded by OCA on Thu Feb 21 13:38:01 2008
