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RETRACTED: GlcNAc‐terminated glycodendrimers form defined precipitates with the soluble dimeric receptor of rat natural killer cells, sNKR‐P1A
Author(s) -
Bezouška Karel,
Křen Vladimír,
Kieburg Christoffer,
Lindhorst Thisbe K
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00340-8
Subject(s) - chemistry , receptor , ligand (biochemistry) , protein subunit , precipitation , stereochemistry , biochemistry , biophysics , crystallography , biology , physics , meteorology , gene
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.