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Jacalin-carbohydrate interactions: distortion of the ligand molecule as a determinant of affinity

Abhinav, KV and Sharma, Kaushal and Swaminathan, CP and Surolia, A and Vijayan, M (2015) Jacalin-carbohydrate interactions: distortion of the ligand molecule as a determinant of affinity. In: ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 71 (2). pp. 324-331.

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Official URL: http://dx.doi.org/ 10.1107/S139900471402553X

Abstract

Jacalin is among the most thoroughly studied lectins. Its carbohydrate-binding site has also been well characterized. It has been postulated that the lower affinity of beta-galactosides for jacalin compared with beta-galactosides is caused by steric interactions of the substituents in the former with the protein. This issue has been explored energetically and structurally using different appropriate carbohydrate complexes of jacalin. It turns out that the earlier postulation is not correct. The interactions of the substituent with the binding site remain essentially the same irrespective of the anomeric nature of the substitution. This is achieved through a distortion of the sugar ring in beta-galactosides. The difference in energy, and therefore in affinity, is caused by a distortion of the sugar ring in beta-galactosides. The elucidation of this unprecedented distortion of the ligand as a strategy for modulating affinity is of general interest. The crystal structures also provide a rationale for the relative affinities of the different carbohydrate ligands for jacalin.

Item Type: Journal Article
Publication: ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
Publisher: WILEY-BLACKWELL
Additional Information: Copy right for this article belongs to the WILEY-BLACKWELL, 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 19 Mar 2015 12:06
Last Modified: 19 Mar 2015 12:06
URI: http://eprints.iisc.ac.in/id/eprint/51035

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