| Type: | Family | Name: | Galectin-1 |
| Description: | Animal lectins are proteins that bind to sugars and are involved in most non-structural roles of sugars, including trafficking of glycoconjugates and cell-cell recognition. Although they may be structurally very complex, they typically bind through the activity of a specific compact protein domain known as a carbohydrate-binding domain or CRD []. Animal lectins display a wide variety of architectures, and are classified according to the carbohydrate-recognition domain (CRD) of which there are two main types, S-type and C-type.Galectins (previously S-lectins) bind exclusively beta-galactosides like lactose. They do not require metal ions for activity. Galectins are found predominantly, but not exclusively in mammals []. Their function is unclear. They are developmentally regulated and may be involved in differentiation, cellular regulation and tissue construction. Mammalian galectins typically bind beta-galactosides. Their CRD shows a structural similarity to L-type lectin CRDs, but no strong sequence similarity, suggesting convergent evolution []. They are classified into three subgroups: proto type, which contain one CRD (Gal-1, -2, -5, -7, -10, -11, -13, -14 and -15); tandem repeat type, which contain two CRDs in tandem (Gal-4, -6, -8, -9 and -12); and chimera type, which contain one CRD and an additional non-lectin domain (Gal-3) [, ].Galectin-1 functions as a dimer with one CRD per monomer, to bind terminal N-acetyllactosamine sequences on extended poly-N-acetyllactosamine (-3Galbeta1-4GlcNAcbeta1-) (n) sequences on cell surfaces []. Galectin-1 has immune regulatory and apoptosis regulatory functions, and has been shown to induce IL-10 production in T-lymphocytes []. | Short Name: | Galectin_1 |
