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Lymphocyte activation receptors: new structural paradigms in group V of C-type animal lectins.

Authors
  • Pavlícek, J
  • Kavan, D
  • Pompach, P
  • Novák, P
  • Luksan, O
  • Bezouska, K
Type
Published Article
Journal
Biochemical Society transactions
Publication Date
Dec 01, 2004
Volume
32
Issue
Pt 6
Pages
1124–1126
Identifiers
PMID: 15506986
Source
Medline
License
Unknown

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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