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Updated: Aug 21, 2026

Antibody Binding Specificity for Kappa (Vκ) Light Chain-containing Human (IgM) Antibodies: Polysialic Acid (PSA) Attached to NCAM as a Case Study
Published on: June 29, 2016
Lymphocyte activation receptors: new structural paradigms in group V of C-type animal lectins
J Pavlícek1, D Kavan, P Pompach
1Department of Biochemistry, Faculty of Science, Charles University, Praha, Czech Republic. pavlicek@biomed.cas.cz
Abstract:
The structure-function relationship in group V of C-type animal lectins remains incompletely understood despite the new structures of NK (natural killer) cell receptors that have been solved recently. Recombinant, soluble forms of rat and human NKR-P1 and CD69 that we obtained after in vitro refolding were analysed by Fourier transform-ion cyclotron resonance MS and heteronuclear NMR ((1)H-(15)N correlation). In NKR-P1, calcium may not be removed by chelating agents because of the very high affinity of binding. In CD69, incorporation of calcium causes a structural shift in several amino acids important for the interaction with carbohydrates. Structural studies have also allowed us to understand an interesting preference of these receptors for either linear (NKR-P1) or branched (CD69) carbohydrate sequences.
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