C-type (Calcium-Dependent, Carbohydrate-Recognition Domain) lectin, Superfamily Member 5

2012 ◽  
pp. 481-481
Author(s):  
Frans van Roy ◽  
Volker Nimmrich ◽  
Anton Bespalov ◽  
Achim Möller ◽  
Hiromitsu Hara ◽  
...  
Keyword(s):  
Carbohydrate Recognition Domain ◽  
Carbohydrate Recognition ◽  
Calcium Dependent

C-type (Calcium-Dependent, Carbohydrate Recognition Domain) Lectin Superfamily Member 9

2012 ◽  
pp. 481-481
Author(s):  
Frans van Roy ◽  
Volker Nimmrich ◽  
Anton Bespalov ◽  
Achim Möller ◽  
Hiromitsu Hara ◽  
...  
Keyword(s):  
Carbohydrate Recognition Domain ◽  
Carbohydrate Recognition ◽  
Calcium Dependent

Genomic analysis of C-type lectins

2002 ◽  
Vol 69 ◽  
pp. 59-72 ◽  
Author(s):  
Kurt Drickamer ◽  
Andrew J. Fadden
Keyword(s):  
Biological Effects ◽  
Cell Signalling ◽  
Genomic Analysis ◽  
Binding Activity ◽  
Immunoglobulin Superfamily ◽  
Carbohydrate Binding ◽  
Carbohydrate Recognition ◽  
Calcium Dependent ◽  
Binding Domains ◽  
Carbohydrate Recognition Domains

Many biological effects of complex carbohydrates are mediated by lectins that contain discrete carbohydrate-recognition domains. At least seven structurally distinct families of carbohydrate-recognition domains are found in lectins that are involved in intracellular trafficking, cell adhesion, cell–cell signalling, glycoprotein turnover and innate immunity. Genome-wide analysis of potential carbohydrate-binding domains is now possible. Two classes of intracellular lectins involved in glycoprotein trafficking are present in yeast, model invertebrates and vertebrates, and two other classes are present in vertebrates only. At the cell surface, calcium-dependent (C-type) lectins and galectins are found in model invertebrates and vertebrates, but not in yeast; immunoglobulin superfamily (I-type) lectins are only found in vertebrates. The evolutionary appearance of different classes of sugar-binding protein modules parallels a development towards more complex oligosaccharides that provide increased opportunities for specific recognition phenomena. An overall picture of the lectins present in humans can now be proposed. Based on our knowledge of the structures of several of the C-type carbohydrate-recognition domains, it is possible to suggest ligand-binding activity that may be associated with novel C-type lectin-like domains identified in a systematic screen of the human genome. Further analysis of the sequences of proteins containing these domains can be used as a basis for proposing potential biological functions.

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