1SLT

STRUCTURE OF S-LECTIN, A DEVELOPMENTALLY REGULATED VERTEBRATE BETA-GALACTOSIDE BINDING PROTEIN

Summary for 1SLT

• Entry DOI: 10.2210/pdb1slt/pdb
• Related PRD ID: PRD_900019
• Descriptor: BOVINE GALECTIN-1, beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: lectin
• Biological source: Bos taurus (cow)
• Total number of polymer chains: 2
• Total formula weight: 30345.16

Authors

Liao, D.-I.,Herzberg, O. (deposition date: 1993-10-20, release date: 1994-01-31, Last modification date: 2020-07-29)

Primary citation

Liao, D.I.,Kapadia, G.,Ahmed, H.,Vasta, G.R.,Herzberg, O.
Structure of S-lectin, a developmentally regulated vertebrate beta-galactoside-binding protein.
Proc.Natl.Acad.Sci.USA, 91:1428-1432, 1994

PubMed Abstract: 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.

PubMed: 8108426
DOI: 10.1073/pnas.91.4.1428

Experimental method

X-RAY DIFFRACTION (1.9 Å)