GlcNAc-terminated glycodendrimers form defined precipitates with the soluble dimeric receptor of rat natural killer cells, sNKR-P1A.
Synthetic GlcNAc-terminated thiourea-bridged glycoclusters were found to be potent inhibitors of binding of the soluble dimeric receptor of rat natural killer cells, sNKR-P1A protein, to its high affinity ligand. Moreover, we have shown here that characteristic precipitation curves can be recorded upon mixing of the GlcNAc glycoclusters with sNKR-P1A. For the GlcNAc8 glycocluster the precipitation curve is biphasic, with high affinity and low affinity precipitates differing in their sensitivity towards GlcNAc-mediated inhibition of precipitation. Quantitative analyses of the precipitates indicate the occurrence of a single sugar binding site per sNKR-P1A subunit, and lead to a model of the most possible spatial arrangements of the glycocluster-receptor lattices. These results provide new tools for further studies on carbohydrate recognition by NKR-P1A.
Bezouska
K
K
Department of Biochemistry, Faculty of Science, Charles University Prague, Phaha, Czech Republic. BEZOUSKA@BIOMED.CAS.CZ
Kren
V
V
Kieburg
C
C
Lindhorst
T K
TK
D000117:Acetylglucosamine / Q000378:metabolism*; D000818:Animals; D000954:Antigens, Surface / Q000737:chemistry / Q000378:metabolism*; D001667:Binding, Competitive; D002240:Carbohydrate Sequence; D011232:Chemical Precipitation; D019281:Dimerization; D006001:Glycoconjugates / Q000737:chemistry / Q000378:metabolism*; D007694:Killer Cells, Natural / Q000378:metabolism*; D037181:Lectins, C-Type; D008024:Ligands; D008362:Mannosides / Q000378:metabolism; D015394:Molecular Structure; D055651:NK Cell Lectin-Like Receptor Subfamily B; D051381:Rats; D012995:Solubility
D000954:Antigens, Surface; D006001:Glycoconjugates; D037181:Lectins, C-Type; D008024:Ligands; D008362:Mannosides; D055651:NK Cell Lectin-Like Receptor Subfamily B; D000117:Acetylglucosamine