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Unusual sugar specificity of banana lectin from Musa paradisiaca andits probable evolutionary origin. Crystallographic and modelling studies

Singh, DD and Saikrishnan, K and Kumar, Prashant and Surolia, A and Sekar, K and Vijayan, M (2005) Unusual sugar specificity of banana lectin from Musa paradisiaca andits probable evolutionary origin. Crystallographic and modelling studies. In: Glycobiology, 15 (10). pp. 1025-1032.

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Abstract

The crystal structure of a complex of methyl-\alpha-D-mannoside with banana lectin from Musa paradisiaca reveals two primary binding sites in the lectin, unlike in other lectins with beta-prism I fold which essentially consists of three Greek key motifs. It has been suggested that the fold evolved through successive gene duplication and fusion of an ancestral Greek key motif. In other lectins, all from dicots, the primary binding site exists on one of the three motifs in the three-fold symmetric molecule. Banana is a monocot, and the three motifs have not diverged enough to obliterate sequence similarity among them. Two Greek key motifs in it carry one primary binding site each. A common secondary binding site exists on the third Greek key. Modelling shows that both the primary sites can support 1-2, 1-3, and 1-6 linked mannosides with the second residue interacting in each case primarily with the secondary binding site. Modelling also readily leads to a bound branched mannopentose with the nonreducing ends of the two branches anchored at the two primary binding sites, providing a structural explanation for the lectin's specificity for branched \alpha-mannans. A comparison of the dimeric banana lectin with other \beta-prism I fold lectins, provides interesting insights into the variability in their quaternary structure.

Item Type: Journal Article
Additional Information: Copyright for this article belongs to Oxford University Press Inc.
Keywords: beta-prism I fold lectin;evolution of carbohydrate specificity;lectin-branched sugar interaction;quaternary association;oligosaccharide modelling
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Division of Information Sciences > Supercomputer Education & Research Centre
Division of Information Sciences > BioInformatics Centre
Date Deposited: 03 Mar 2006
Last Modified: 19 Sep 2010 04:20
URI: http://eprints.iisc.ernet.in/id/eprint/3880

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