Please use this identifier to cite or link to this item:
Title: Binding of sucrose octasulphate to the C-type lectin-like domain of the recombinant natural killer cell receptor NKR-P1A observed by NMR spectroscopy.
Authors: Kogelberg, H
Frenkiel, TA
Birdsall, B
Chai, W
Muskett, FW
First Published: 4-Nov-2002
Citation: CHEMBIOCHEM, 2002, 3 (11), pp. 1072-1077
Abstract: NKR-P1A is a C-type lectin-like receptor on natural killer cells believed to be involved in the cytotoxicity of these cells. Ligands for this protein are not known. Here, we describe the binding of a fully sulphated disaccharide, sucrose octasulphate, by the recombinant C-type lectin-like domain of NKR-P1A. The binding was observed by NMR spectroscopy methods that have recently been described for the screening of compound libraries for bioaffinities, namely the 2D NOESY and saturation transfer difference NMR experiments. (1)H titration studies indicate that the binding is specific. These findings raise the possibility that NKR-P1A recognises sulphated natural ligands in common with certain other members of the C-type lectin family.
DOI Link: 10.1002/1439-7633(20021104)3:11<1072::AID-CBIC1072>3.0.CO;2-1
ISSN: 1439-4227
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Biochemistry

Files in This Item:
There are no files associated with this item.

Items in LRA are protected by copyright, with all rights reserved, unless otherwise indicated.