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 (1H-15N 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.
Lymphocyte activation receptors: new structural paradigms in group V of C-type animal lectins
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J. Pavlíček, D. Kavan, P. Pompach, P. Novák, O. Lukšan, K. Bezouška; Lymphocyte activation receptors: new structural paradigms in group V of C-type animal lectins. Biochem Soc Trans 1 November 2004; 32 (6): 1124–1126. doi: https://doi.org/10.1042/BST0321124
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