Specificity of C-Glycoside Complexation by Mannose/Glucose Specific Lectins
| Autor: | Mary C. Chervenak, Kathleen H. Mortell, Laura L. Kiessling, Eric J. Toone, Ross V. Weatherman |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
biology
Chemistry Lectin Mannose Calorimetry Ligands biology.organism_classification Canavalia Biochemistry Monosaccharide binding Dioclea grandiflora Structure-Activity Relationship chemistry.chemical_compound Glucosides Concanavalin A Lectins Mannosides Canavalia ensiformis biology.protein Plant Lectins Binding site Protein Binding |
| Zdroj: | Biochemistry. 35:3619-3624 |
| ISSN: | 1520-4995 0006-2960 |
| Popis: | The binding of the mannose/glucose specific lectins from Canavalia ensiformis (concanavalin A) and Dioclea grandiflora to a series of C-glucosides were studied by titration microcalorimetry and fluorescence anisotropy titration. These closely related lectins share a specificity for the trimannoside methyl 3,6-di-O-(alpha-D-mannopyranosyl)-alpha-D-mannopyranoside, and are a useful model system for addressing the feasibility of differentiating between lectins with overlapping carbohydrate specificities. The ligands were designed to address two issues: (1) how the recognition properties of non-hydrolyzable C-glycoside analogues compare with those of the corresponding O-glycosides and (2) the effect of presentation of more than one saccharide recognition epitope on both affinity and specificity. Both lectins bind the C-glycosides with affinities comparable to those of the O-glycoside analogues; however, the ability of both lectins to differentiate between gluco and manno diastereomers was diminished in the C-glycoside series. Bivalent norbornyl C-glycoside esters were bound by the lectin from Canavalia but only weakly by the lectin from Dioclea. In addition to binding the bivalent ligands, concanavalin A discriminated between C-2 epimers, with the manno configuration binding more tightly than the gluco. The stoichiometry of binding of the bivalent ligands to both di- and tetrameric lectin was two binding sites per ligand, rather than the expected 1:1 stoichiometry. Together, these results suggest that concanavalin A may possess more than one class of carbohydrate binding sites and that these additional sites show stereochemical discrimination similar to that of the previously identified monosaccharide binding site. The implications of these findings for possible in vivo roles of plant lectins and for the use of concanavalin A as a research tool are discussed. |
| Databáze: | OpenAIRE |
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