1slt

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(New page: 200px<br /><applet load="1slt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1slt, resolution 1.9&Aring;" /> '''STRUCTURE OF S-LECTIN...)
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Revision as of 00:21, 21 November 2007

Image:1slt.jpg

1slt, resolution 1.9Å

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

Overview

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 Structure

1SLT is a Single protein structure of sequence from [1] with CL and CYO as ligands. Full crystallographic information is available from OCA.

Reference

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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