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- W2010631191 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 (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." @default.
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- W2010631191 date "2004-10-26" @default.
- W2010631191 modified "2023-10-04" @default.
- W2010631191 title "Lymphocyte activation receptors: new structural paradigms in group V of C-type animal lectins" @default.
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- W2010631191 doi "https://doi.org/10.1042/bst0321124" @default.
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