1slt
STRUCTURE OF S-LECTIN, A DEVELOPMENTALLY REGULATED VERTEBRATE BETA-GALACTOSIDE BINDING PROTEIN
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| , resolution 1.9Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
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.
About this StructureAbout this Structure
1SLT is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
ReferenceReference
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
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