Revisiting legume lectins: Structural organization and carbohydrate-binding properties.

Autor: Osterne VJS; Laboratory of Biochemistry and Glycobiology, Department of Biotechnology, Ghent University, Proeftuinstraat 86, 9000, Ghent, Belgium., De Sloover G; Laboratory of Biochemistry and Glycobiology, Department of Biotechnology, Ghent University, Proeftuinstraat 86, 9000, Ghent, Belgium., Van Damme EJM; Laboratory of Biochemistry and Glycobiology, Department of Biotechnology, Ghent University, Proeftuinstraat 86, 9000, Ghent, Belgium. Electronic address: ElsJM.VanDamme@UGent.be.
Jazyk: angličtina
Zdroj: Carbohydrate research [Carbohydr Res] 2024 Oct; Vol. 544, pp. 109241. Date of Electronic Publication: 2024 Aug 13.
DOI: 10.1016/j.carres.2024.109241
Abstrakt: Legume lectins are a diverse family of carbohydrate-binding proteins that share significant similarities in their primary, secondary, and tertiary structures, yet exhibit remarkable variability in their quaternary structures and carbohydrate-binding specificities. The tertiary structure of legume lectins, characterized by a conserved β-sandwich fold, provides the scaffold for the formation of a carbohydrate-recognition domain (CRD) responsible for ligand binding. The structural basis for the binding is similar between members of the family, with key residues interacting with the sugar through hydrogen bonds, hydrophobic interactions, and van der Waals forces. Variability in substructures and residues within the CRD are responsible for the large array of specificities and enable legume lectins to recognize diverse sugar structures, while maintaining a consistent structural fold. Therefore, legume lectins can be classified into several specificity groups based on their preferred ligands, including mannose/glucose-specific, N-acetyl-d-galactosamine/galactose-specific, N-acetyl-d-glucosamine-specific, l-fucose-specific, and α-2,3 sialic acid-specific lectins. In this context, this review examined the structural aspects and carbohydrate-binding properties of representative legume lectins and their specific ligands in detail. Understanding the structure/binding relationships of lectins continues to provide valuable insights into their biological roles, while also assisting in the potential applications of these proteins in glycobiology, diagnostics, and therapeutics.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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