GlcNAc-terminated glycodendrimers form defined precipitates with the soluble dimeric receptor of rat natural killer cells, sNKR-P1A
Language English Country Great Britain, England Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
9599017
DOI
10.1016/s0014-5793(98)00340-8
PII: S0014-5793(98)00340-8
Knihovny.cz E-resources
- MeSH
- Acetylglucosamine metabolism MeSH
- Antigens, Surface chemistry metabolism MeSH
- Killer Cells, Natural metabolism MeSH
- Chemical Precipitation MeSH
- Dimerization MeSH
- Glycoconjugates chemistry metabolism MeSH
- Binding, Competitive MeSH
- Rats MeSH
- NK Cell Lectin-Like Receptor Subfamily B MeSH
- Lectins, C-Type * MeSH
- Ligands MeSH
- Mannosides metabolism MeSH
- Molecular Structure MeSH
- Solubility MeSH
- Carbohydrate Sequence MeSH
- Animals MeSH
- Check Tag
- Rats MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Acetylglucosamine MeSH
- Antigens, Surface MeSH
- Glycoconjugates MeSH
- NK Cell Lectin-Like Receptor Subfamily B MeSH
- Lectins, C-Type * MeSH
- Ligands MeSH
- Mannosides MeSH
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.
References provided by Crossref.org
Nkrp1 family, from lectins to protein interacting molecules
