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Structural studies on peanut lectin complexed with disaccharides involving different linkages: further insights into the structure and interactions of the lectin.

Natchiar SK, Srinivas O, Mitra N, Surolia A, Jayaraman N, Vijayan M
Acta Crystallogr D Biol Crystallogr 62 1413-21 (2006)
Related entries: 1v6i, 1v6j, 1v6k, 1v6l, 1v6m, 1v6n, 1v6o, 2dv9, 2dvb, 2dvd, 2dvf, 2dvg, 2pel

Cited: 18 times
EuropePMC logo PMID: 17057347

Abstract

Crystal structures of peanut lectin complexed with Galbeta1-3Gal, methyl-T-antigen, Galbeta1-6GalNAc, Galalpha1-3Gal and Galalpha1-6Glc and that of a crystal grown in the presence of Galalpha1-3Galbeta1-4Gal have been determined using data collected at 100 K. The use of water bridges as a strategy for generating carbohydrate specificity was previously deduced from the complexes of the lectin with lactose (Galbeta1-4Glc) and T-antigen (Galbeta1-3GalNAc). This has been confirmed by the analysis of the complexes with Galbeta1-3Gal and methyl-T-antigen (Galbeta1-3GalNAc-alpha-OMe). A detailed analysis of lectin-sugar interactions in the complexes shows that they are more extensive when the beta-anomer is involved in the linkage. As expected, the second sugar residue is ill-defined when the linkage is 1-->6. There are more than two dozen water molecules which occur in the hydration shells of all structures determined at resolutions better than 2.5 A. Most of them are involved in stabilizing the structure, particularly loops. Water molecules involved in lectin-sugar interactions are also substantially conserved. The lectin molecule is fairly rigid and does not appear to be affected by changes in temperature.

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  2. Structural biology of carbohydrate xenoantigens. Yuriev E, Agostino M, Farrugia W, Christiansen D, Sandrin MS, Ramsland PA. Expert Opin Biol Ther 9 1017-1029 (2009)
  3. Glycosylated gold nanoparticles in point of care diagnostics: from aggregation to lateral flow. Baker AN, Hawker-Bond GW, Georgiou PG, Dedola S, Field RA, Gibson MI. Chem Soc Rev 51 7238-7259 (2022)

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