Structural highlights
Function
[LEG1_BOVIN] May regulate apoptosis, cell proliferation and cell differentiation. Binds beta-galactoside and a wide array of complex carbohydrates. Inhibits CD45 protein phosphatase activity (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of a 14-kDa bovine spleen S-lectin complexed with the disaccharide N-acetyllactosamine at 1.9-A resolution reveals a surprising structural relationship to legume lectins, despite the lack of sequence homology. Two monomers associate to form an extended beta-sandwich, each with the same jelly roll topology typical of legume lectins but with dramatically trimmed loops and with different dimer association. Each monomer binds one N-acetyllactosamine molecule in a topologically and spatially different site than that of legume lectins. The carbohydrate-binding site provides an unprecedented paradigm for carbohydrate binding, with a unique network of salt bridges. The specificity for beta-galactose arises from intricate interactions that constrain the position of the O4 atom.
Structure of S-lectin, a developmentally regulated vertebrate beta-galactoside-binding protein.,Liao DI, Kapadia G, Ahmed H, Vasta GR, Herzberg O Proc Natl Acad Sci U S A. 1994 Feb 15;91(4):1428-32. PMID:8108426[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Liao DI, Kapadia G, Ahmed H, Vasta GR, Herzberg O. Structure of S-lectin, a developmentally regulated vertebrate beta-galactoside-binding protein. Proc Natl Acad Sci U S A. 1994 Feb 15;91(4):1428-32. PMID:8108426
