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Varki A, Cummings RD, Esko JD, et al., editors. Essentials of Glycobiology [Internet]. 3rd edition. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 2015-2017.
Essentials of Glycobiology [Internet]. 3rd edition.
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Table 1
| Features | Lectinsa | Glycosaminoglycan-binding proteinsb |
|---|---|---|
| Shared evolutionary origins | yes (within each group) | no |
| Shared structural features | yes (within each group) | no |
| Defining amino acid residues involved in binding | often typical for each group | patch of basic amino acid residues |
| Type of glycans recognized | N-glycans, O-glycans, glycosphingolipids (a few also recognize sulfated glycosaminoglycans) | different types of sulfated glycosaminoglycans |
| Location of cognate residues within glycans | typically in sequences at outer ends of glycan chains | typically in sequences internal to an extended sulfated glycosaminoglycan chain |
| Specificity for glycans recognized | stereospecificity high for specific glycan structures | often recognize a range of related sulfated glycosaminoglycan structures |
| Single-site binding affinity | often low; high avidity generated by multivalency | often moderate to high |
| Valency of binding sites | multivalency common (either within native structure or by clustering) | often monovalent |
| Subgroups | C-type lectins, galectins, P-type lectins, I-type lectins, L-type lectins, R-type lectins, etc. | heparan sulfate–binding proteins, chondroitin sulfate–binding proteins, dermatan sulfate–binding proteins |
| Types of glycans recognized within each group | can be similar (e.g., galectins) or variable (e.g., C-type lectins) | classification itself is based on type of glycosaminoglycan chain recognized |
Modified from Varki A, Angata T. 2006. Glycobiology 16: 1R–27R.
- a
There are other animal proteins that recognize glycans in a lectin-like manner and do not appear to fall into one of the well-recognized classes (e.g., various cytokines).
- b
Hyaluronan (HA)-binding proteins (hyaloadherins) fall in between these two classes. On the one hand, some (but not all) of the hyaloadherins have shared evolutionary origins. On the other hand, recognition involves internal regions of HA, which is a nonsulfated glycosaminoglycan.
- Comparison of Two Major Classes of Glycan-Binding Proteins - Essentials of Glyco...Comparison of Two Major Classes of Glycan-Binding Proteins - Essentials of Glycobiology
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