The insecticidal activity of carbohydrate-binding plant lectins against insects belonging to coleoptera, diptera, lepidoptera and homoptera have been amply investigated [ 20- 25].
Therefore, in terms of carbohydrate-binding activity, L5 should be the predominant structural element for high binding activity, and the N- and C-terminal regions may play an auxiliary role in carbohydrate binding by increasing the structural stability or slightly altering the structure.
Biochemical analysis of BiXyn10A demonstrated that such insertion sequences encode a new family of carbohydrate-binding modules (CBMs) that binds to xylose-configured oligosaccharide/polysaccharide ligands, the substrate of the BiXyn10A enzymatic activity.
The current model suggests glycoside hydrolase activities are lost though non-specific/non-productive binding of carbohydrate-binding domains to lignin, limiting catalytic site access to the carbohydrate components of the cell wall.
Our results suggest that DUF26-containing proteins constitute a group of carbohydrate-binding proteins in plants.
The occurrence of carbohydrate-binding proteins in all kingdoms of life illustrates their importance.
Carbohydrate-binding proteins, known as lectins, exhibit a range of carbohydrate-binding specificities.
Lectins are a class of carbohydrate-binding proteins.
Sugar-binding receptors of the C-type lectin family contain structurally related carbohydrate recognition domains (CRDs) but display a diversity of carbohydrate-binding specificities (Weis et al. 1998).
Iduna is a PAR polymer-binding protein, and mutation at the PAR polymer binding site abolishes the PAR binding activity of Iduna and attenuates its protective actions.
