title: New structural insights into lectin-type proteins of the immune system.
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.
authors.affiliation: 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
authors.forename: H
authors.initials: H
authors.lastname: Kogelberg
authors.forename: T
authors.initials: T
authors.lastname: Feizi
mesh_terms: D000818:Animals; D001665:Binding Sites; D015815:Cell Adhesion Molecules / Q000737:chemistry; D006801:Humans; D007694:Killer Cells, Natural / Q000276:immunology; D037102:Lectins / Q000737:chemistry*; D008024:Ligands; D046911:Macromolecular Substances; D008958:Models, Molecular; D015394:Molecular Structure; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000276:immunology*; D011971:Receptors, Immunologic / Q000737:chemistry; D019087:Selectins / Q000737:chemistry; D001619:beta-N-Acetylhexosaminidases
chemical_list: D015815:Cell Adhesion Molecules; D037102:Lectins; D008024:Ligands; D046911:Macromolecular Substances; D011506:Proteins; D011971:Receptors, Immunologic; D019087:Selectins; C072273:TNFAIP6 protein, human; C513057:Tnfaip6 protein, mouse; C429541:Chil3 protein, mouse; D001619:beta-N-Acetylhexosaminidases