Lymphocyte activation receptors: new structural paradigms in group V of C-type animal lectins. (26th October 2004)

• Record Type: Journal Article
• Authors: Pavlíček, J.; Kavan, D.; Pompach, P.; Novák, P.; Lukšan, O.; Bezouška, K.
• Is Part Of: Biochemical Society transactions. Volume 32:Number 6(2004)
• Page Start: 1124
• Page End: 1126
• Publication Date: 2004-10-26
• Subjects: lectin-type receptor -- ligand identification -- lymphocyte -- natural killing; Biochemistry -- Congresses; 572
• DOI: 10.1042/BST0321124
• Languages: English
• ISSNs: 0300-5127

Abstract

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.