Title : Binding of N-acetylglucosamine (GlcNAc) β1-6-branched oligosaccharide acceptors to β4-galactosyltransferase I reveals a new ligand binding mode.

Pub. Date : 2012 Aug 17

PMID : 22740701






3 Functional Relationships(s)
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1 In the crystal structure of the complex of beta4Gal-T1 with I-antigen analog pentasaccharide, the beta1-6-branched GlcNAc moiety is bound to the sugar acceptor binding site of the beta4Gal-T1 molecule in a way similar to the crystal structures described previously; however, the extended linear tetrasaccharide moiety does not interact with the previously found extended sugar binding site on the beta4Gal-T1 molecule. pentasaccharide beta-1,4-galactosyltransferase 1 Homo sapiens
2 In the crystal structure of the complex of beta4Gal-T1 with I-antigen analog pentasaccharide, the beta1-6-branched GlcNAc moiety is bound to the sugar acceptor binding site of the beta4Gal-T1 molecule in a way similar to the crystal structures described previously; however, the extended linear tetrasaccharide moiety does not interact with the previously found extended sugar binding site on the beta4Gal-T1 molecule. pentasaccharide beta-1,4-galactosyltransferase 1 Homo sapiens
3 In the crystal structure of the complex of beta4Gal-T1 with I-antigen analog pentasaccharide, the beta1-6-branched GlcNAc moiety is bound to the sugar acceptor binding site of the beta4Gal-T1 molecule in a way similar to the crystal structures described previously; however, the extended linear tetrasaccharide moiety does not interact with the previously found extended sugar binding site on the beta4Gal-T1 molecule. pentasaccharide beta-1,4-galactosyltransferase 1 Homo sapiens