Recent insights into structures and functions of C-type lectins in the immune system
| Autor: | Maureen E. Taylor, Kurt Drickamer |
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| Rok vydání: | 2015 |
| Předmět: |
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Molecular Glycosylation Protein Conformation Endocytic cycle Plasma protein binding Biology Ligands Article Structure-Activity Relationship chemistry.chemical_compound Immune system Species Specificity Structural Biology Animals Humans Lectins C-Type Receptor Molecular Biology Innate immune system Cell biology chemistry Immune System Protein Multimerization Signal transduction Function (biology) Protein Binding Signal Transduction |
| Zdroj: | Current Opinion in Structural Biology |
| ISSN: | 0959-440X |
| DOI: | 10.1016/j.sbi.2015.06.003 |
| Popis: | Highlights • Sugar-binding C-type carbohydrate-recognition domains fall in five structural groups. • Structures for many of these domains, covering all of the groups, have been obtained. • Not all human C-type lectins have clear orthologues in other mammals such as mice. • Different mechanisms by which C-type lectins initiate signalling remain to be defined. • Hetero-oligomeric receptors add to the complexity of overlapping specificities. 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. |
| Databáze: | OpenAIRE |
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