2dty › Citations

Structural basis for the carbohydrate-specificity of basic winged-bean lectin and its differential affinity for Gal and GalNAc.

Kulkarni KA, Katiyar S, Surolia A, Vijayan M, Suguna K
Acta Crystallogr D Biol Crystallogr 62 1319-24 (2006)
Related entries: 1wbf, 1wbl, 2d3s, 2dtw, 2du0, 2du1

Cited: 2 times
EuropePMC logo PMID: 17057334

Abstract

The crystal structure of the complexes of basic winged-bean lectin with galactose, 2-methoxygalactose, N-acetylgalactosamine and methyl-alpha-N-acetylgalactosamine have been determined. Lectin-sugar interactions involve four hydrogen bonds and a stacking interaction in all of the complexes. In addition, an N-H...O hydrogen bond involving the hydroxyl group at C2 exists in the galactose and 2-methoxygalactose complexes. An additional hydrophobic interaction involving the methyl group in the latter leads to the higher affinity of the methyl derivative. In the lectin-N-acetylgalactosamine complex the N-H...O hydrogen bond is lost, but a compensatory hydrogen bond is formed involving the O atom of the acetamido group. In addition, the CH(3) moiety of the acetamido group is involved in hydrophobic interactions. Consequently, the 2-methyl and acetamido derivatives of galactose have nearly the same affinity for the lectin. The methyl group alpha-linked to the galactose takes part in additional hydrophobic interactions. Therefore, methyl-alpha-N-acetylgalactosamine has a higher affinity than N-acetylgalactosamine for the lectin. The structures of basic winged-bean lectin-sugar complexes provide a framework for examining the relative affinity of galactose and galactosamine for the lectins that bind to them. The complexes also lead to a structural explanation for the blood-group specificity of basic winged-bean lectin.

Articles citing this publication (2)

  1. Generation of blood group specificity: new insights from structural studies on the complexes of A- and B-reactive saccharides with basic winged bean agglutinin. Kulkarni KA, Katiyar S, Surolia A, Vijayan M, Suguna K. Proteins 68 762-769 (2007)
  2. Metagenomics-based systematic analysis reveals that gut microbiota Gd-IgA1-associated enzymes may play a key role in IgA nephropathy. Liang X, Zhang S, Zhang D, Hu L, Zhang, Peng Y, Xu Y, Hou H, Zou C, Liu X, Chen Y, Lu F. Front Mol Biosci 9 970723 (2022)


Related citations provided by authors (3)

  1. Carbohydrate specificity and quaternary association in basic winged bean lectin: X-ray analysis of the lectin at 2.5 A resolution.. Prabu MM, Sankaranarayanan R, Puri KD, Sharma V, Surolia A, Vijayan M, Suguna K J Mol Biol 276 787-96 (1998)
  2. Structural basis for the specificity of basic winged bean lectin for the Tn-antigen: a crystallographic, thermodynamic and modelling study.. Kulkarni KA, Sinha S, Katiyar S, Surolia A, Vijayan M, Suguna K FEBS Lett 579 6775-80 (2005)
  3. Structure of basic winged-bean lectin and a comparison with its saccharide-bound form.. Manoj N, Srinivas VR, Suguna K Acta Crystallogr D Biol Crystallogr 55 794-800 (1999)

Quick links