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Curr Opin Struct Biol. 2001 Oct;11(5):635-43.

New structural insights into lectin-type proteins of the immune system.

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1
The Glycosciences Laboratory, Faculty of Medicine, Imperial College of Science, Technology and Medicine, Northwick Park Institute for Medical Research, Harrow, Middlesex, UK. h.kogelberg@ic.ac.uk

Abstract

New structural data have emerged for the ligand-binding sites of C-type lectin domains and C-type lectin-like domains of receptors of the immune system. These include binding sites for oligosaccharide or polypeptide ligands, or both oligosaccharide and polypeptide ligands. The structural basis for the binding of a lectin domain of the beta-trefoil family to different sulfooligosaccharide sequences has been revealed. Lectin activity has been documented for a beta/alpha TIM barrel fold that does not have the chitinase activity of the prototype enzyme with this fold.

PMID:
11785767
[Indexed for MEDLINE]
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