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1slc
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(New page: 200px<br /><applet load="1slc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1slc, resolution 2.15Å" /> '''X-RAY CRYSTALLOGRAPH...)
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Revision as of 00:20, 21 November 2007
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X-RAY CRYSTALLOGRAPHY REVEALS CROSSLINKING OF MAMMALIAN LECTIN (GALECTIN-1) BY BIANTENNARY COMPLEX TYPE SACCHARIDES
Overview
Galectins are beta-galactoside-binding proteins that occur intra- and, extracellularly in many animal tissues. They have been proposed to form, networks of glycoconjugates on the cell surface, where they may modulate, various cell response pathways such as growth, activation and adhesion., The high resolution X-ray crystallographic analyses of three crystal forms, of bovine galectin-1 in complex with biantennary saccharides of, N-acetyllactosamine type reveal infinite chains of lectin dimers, cross-linked through N-acetyllactosamine units located at the end of the, oligosaccharide antenna. The oligosaccharide adopts a different low energy, conformation in each of the three crystal forms.
About this Structure
1SLC is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Crosslinking of mammalian lectin (galectin-1) by complex biantennary saccharides., Bourne Y, Bolgiano B, Liao DI, Strecker G, Cantau P, Herzberg O, Feizi T, Cambillau C, Nat Struct Biol. 1994 Dec;1(12):863-70. PMID:7773775
Page seeded by OCA on Wed Nov 21 02:27:32 2007
