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Proc Natl Acad Sci U S A. 1994 Feb 15;91(4):1428-32.

Structure of S-lectin, a developmentally regulated vertebrate beta-galactoside-binding protein.

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  • 1Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, Rockville 20850.


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.

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