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Comparative Studies of Vertebrate Platelet Glycoprotein 4 (CD36)

Promiscuity of the Euonymus Carbohydrate-Binding Domain

Laboratory of Biochemistry and Glycobiology, Department of Molecular Biotechnology, Ghent University, Coupure links 653, 9000 Ghent, Belgium
Author to whom correspondence should be addressed.
Biomolecules 2012, 2(4), 415-434;
Received: 23 August 2012 / Revised: 17 September 2012 / Accepted: 25 September 2012 / Published: 8 October 2012
(This article belongs to the Special Issue Challenges in Glycan, Glycoprotein and Proteoglycan Research)
Plants synthesize small amounts of carbohydrate-binding proteins on exposure to stress. For example, on exposure to drought, high salt, wounding and by treatment with some plant hormones or by pathogen attack. In contrast to the ‘classical’ plant lectins that are mostly located in the vacuolar compartment, this new class of inducible lectins is present in the cytoplasm and in the nucleus. Taking into account that any physiological role of plant lectins most likely relies on their specific carbohydrate-binding activity and specificity, the discovery of these stress-related lectins provides strong evidence for the importance of protein-carbohydrate-interactions in plant cells. Hitherto, six families of such nucleocytoplasmic lectins have been identified in plants. This review will focus on the nucleocytoplasmic lectins with one or more Euonymus lectin (EUL) domain(s). The carbohydrate-binding specificity of EUL proteins from a monocot, a dicot and a lower plant has been compared. Furthermore, modeling of the different EUL domains revealed a similar ß-trefoil fold consisting of three bundles of ß-sheet organized around a pseudo three-fold symmetry axis. Despite the sequence similarity and the conserved amino acids in the binding site, glycan array analyses showed that the EUL domain has a promiscuous carbohydrate-binding site capable of accommodating high mannose N-glycans, blood group B related structures and galactosylated epitopes. View Full-Text
Keywords: binding site; carbohydrate; cytoplasm; lectin; nucleus; specificity binding site; carbohydrate; cytoplasm; lectin; nucleus; specificity
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MDPI and ACS Style

Fouquaert, E.; Van Damme, E.J.M. Promiscuity of the Euonymus Carbohydrate-Binding Domain. Biomolecules 2012, 2, 415-434.

AMA Style

Fouquaert E, Van Damme EJM. Promiscuity of the Euonymus Carbohydrate-Binding Domain. Biomolecules. 2012; 2(4):415-434.

Chicago/Turabian Style

Fouquaert, Elke, and Els J.M. Van Damme. 2012. "Promiscuity of the Euonymus Carbohydrate-Binding Domain" Biomolecules 2, no. 4: 415-434.

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