title: Recent insights into structures and functions of C-type lectins in the immune system.
abstract: The majority of the C-type lectin-like domains in the human genome likely to bind sugars have been investigated structurally, although novel mechanisms of sugar binding are still being discovered. In the immune system, adhesion and endocytic receptors that bind endogenous mammalian glycans are often conserved, while pathogen-binding C-type lectins on cells of the innate immune system are more divergent. Lack of orthology between some human and mouse receptors, as well as overlapping specificities of many receptors and formation of receptor hetero-oligomers, can make it difficult to define the roles of individual receptors. There is good evidence that C-type lectins initiate signalling pathways in several different ways, but this function remains the least well understood from a mechanistic perspective.
authors.affiliation: Department of Life Sciences, Imperial College, London SW7 2AZ, United Kingdom.
authors.forename: Kurt
authors.initials: K
authors.lastname: Drickamer
authors.affiliation: Department of Life Sciences, Imperial College, London SW7 2AZ, United Kingdom. Electronic address: maureen.taylor@imperial.ac.uk.
authors.forename: Maureen E
authors.initials: ME
authors.lastname: Taylor
mesh_terms: D000818:Animals; D006031:Glycosylation; D006801:Humans; D007107:Immune System / Q000502:physiology*; D037181:Lectins, C-Type / Q000737:chemistry* / Q000145:classification / Q000378:metabolism*; D008024:Ligands; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D055503:Protein Multimerization; D015398:Signal Transduction; D013045:Species Specificity; D013329:Structure-Activity Relationship
chemical_list: D037181:Lectins, C-Type; D008024:Ligands