Lymphocyte activation receptors: new structural paradigms in group V of C-type animal lectins.
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.
Pavlícek
J
J
Department of Biochemistry, Faculty of Science, Charles University, Praha, Czech Republic. pavlicek@biomed.cas.cz
Kavan
D
D
Pompach
P
P
Novák
P
P
Luksan
O
O
Bezouska
K
K
D000595:Amino Acid Sequence; D000818:Animals; D015703:Antigens, CD / Q000276:immunology; D000945:Antigens, Differentiation, T-Lymphocyte / Q000276:immunology; D006801:Humans; D007694:Killer Cells, Natural / Q000276:immunology; D037181:Lectins, C-Type / Q000737:chemistry / Q000502:physiology*; D008213:Lymphocyte Activation / Q000276:immunology*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D011487:Protein Conformation; D051381:Rats; D000099192:CD69 Antigens
D015703:Antigens, CD; D000945:Antigens, Differentiation, T-Lymphocyte; D037181:Lectins, C-Type; D000099192:CD69 Antigens