1a78

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Revision as of 11:32, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1a78" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a78, resolution 2.0Å" /> '''COMPLEX OF TOAD OVARY...)
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File:1a78.jpg


1a78, resolution 2.0Å

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COMPLEX OF TOAD OVARY GALECTIN WITH THIO-DIGALACTOSE

OverviewOverview

Galectin-1, S-type beta-galactosyl-binding lectins present in vertebrate, and invertebrate species, are dimeric proteins that participate in, cellular adhesion, activation, growth regulation, and apoptosis. Two, high-resolution crystal structures of B. arenarum galectin-1 in complex, with two related carbohydrates, LacNAc and TDG, show that the, topologically equivalent hydroxyl groups in the two disaccharides exhibit, identical patterns of interaction with the protein. Groups that are not, equivalent between the two sugars present in the second moiety of the, disaccharide, interact differently with the protein, but use the same, number and quality of interactions. The structures show additional, protein-carbohydrate interactions not present in previously reported, lectin-lactose complexes. These contacts provide an explanation for the, enhanced affinity of galectin-1 for TDG and LacNAc relative to lactose., Galectins are in dimer-monomer equilibrium at physiological protein, concentrations, suggesting that this equilibrium may be involved in, organ-specific regulation of activity. Comparison of B. arenarum with, other galectin-1 structures shows that among different galectins there are, significant changes in accessible surface area buried upon dimer, formation, providing a rationale for the variations observed in the, free-energies of dimerization. The structure of the B. arenarum galectin-1, has a large cleft with a strong negative potential that connects the two, binding sites at the surface of the protein. Such a striking, characteristic suggests that this cleft is probably involved in, interactions of the galectin with other intra or extra-cellular proteins., Proteins 2000;40:378-388.

About this StructureAbout this Structure

1A78 is a Single protein structure of sequence from Bufo arenarum with TDG and DTT as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Soluble beta-galactosyl-binding lectin (galectin) from toad ovary: crystallographic studies of two protein-sugar complexes., Bianchet MA, Ahmed H, Vasta GR, Amzel LM, Proteins. 2000 Aug 15;40(3):378-88. PMID:10861929

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