|SMART accession number:||SM00276|
|Description:||Galectin - galactose-binding lectin|
|Interpro abstract (IPR001079):|
Galectins (also known as galaptins or S-lectin) are a family of proteins defined by having at least one characteristic carbohydrate recognition domain (CRD) with an affinity for beta-galactosides and sharing certain sequence elements. Members of the galectins family are found in mammals, birds, amphibians, fish, nematodes, sponges, and some fungi. Galectins are known to carry out intra- and extracellular functions through glycoconjugate-mediated recogntion. From the cytosol they may be secreted by non-classical pathways, but they may also be targeted to the nucleus or specific sub-cytosolic sites. Within the same peptide chain some galectins have a CRD with only a few additional amino acids, whereas others have two CRDs joined by a link peptide, and one (galectin-3) has one CRD joined to a different type of domain [(PUBMED:16051274), (PUBMED:14758066)].
The galectin carbohydrate recognition domain (CRD) is a beta-sandwich of about 135 amino acid. The two sheets are slightly bent with 6 strands forming the concave side and 5 strands forming the convex side. The concave side forms a groove in which carbohydrate is bound, and which is long enough to hold about a linear tetrasaccharide [(PUBMED:8262940), (PUBMED:8747464)].
|GO function:||carbohydrate binding (GO:0030246)|
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- Evolution (species in which this domain is found)
- Metabolism (metabolic pathways involving proteins which contain this domain)
- Structure (3D structures containing this domain)
- Links (links to other resources describing this domain)