Carbohydrate-Recognition Proteins of Macrophages and Related Cells

1993 ◽  
pp. 347-370
Author(s):  
Maureen E. Taylor
Keyword(s):  
Carbohydrate Recognition

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.

scholarly journals Binding modes of methyl α-d-glucopyranoside to an artificial receptor in crystalline complexes

RSC Advances ◽  
2021 ◽  
Vol 11 (36) ◽  
pp. 22221-22229
Author(s):  
Linda Köhler ◽  
Conrad Hübler ◽  
Wilhelm Seichter ◽  
Monika Mazik
Keyword(s):  
Binding Modes ◽  
Carbohydrate Recognition ◽  
Valuable Source ◽  
Molecular Features ◽  
Artificial Receptor ◽  
Source Of Information

Complexes formed between methyl α-d-glucopyranoside and an artificial receptor represent a valuable source of information about the basic molecular features of carbohydrate recognition.

Cholesteryl glucosides signal through the carbohydrate recognition domain of the macrophage inducible C-type lectin (mincle)

2021 ◽  
Author(s):  
Mattie S. M. Timmer ◽  
Thomas J. Teunissen ◽  
Kristel Kodar ◽  
Amy J. Foster ◽  
Sho Yamasaki ◽  
...  
Keyword(s):  
Carbohydrate Recognition Domain ◽  
Carbohydrate Recognition ◽  
H Pylori

H. pylori derived cholesteryl glycosides signal through the Carbohydrate Recognition Domain (CRD) of the Macrophage inducible C-type lectin (Mincle).

scholarly journals The role of carbohydrate recognition during human sperm-egg binding

2013 ◽  
Vol 28 (3) ◽  
pp. 566-577 ◽  
Author(s):  
G. F. Clark
Keyword(s):  
Human Sperm ◽  
Carbohydrate Recognition

Overcoming Degeneracy in Carbohydrate Recognition

2003 ◽  
Vol 42 (22) ◽  
pp. 2504-2506 ◽  
Author(s):  
Amit Basu ◽  
Daniel Kahne
Keyword(s):  
Carbohydrate Recognition
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