Glycobiology Advance Access published online on January 22, 2003
Glycobiology, doi:10.1093/glycob/cwg042
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© 2003 Oxford University Press
ORIGINAL ARTICLES
1 Centre de Recherches sur les Macromolécules Végétales, CNRS (affiliated with Université Joseph Fourier), BP 53, 38041 Grenoble cedex 9, France; Institute of Chemical Technology, Technická 5, 166 28 Prague, Czech Republic A terminal
Revised on December 9, 2002
Accepted on December 17, 2002
Molecular modeling of glycosyltransferases involved in the biosynthesis of blood group A, blood group B, Forssman and iGb3 antigens and their interaction with substrates
2 Centre de Recherches sur les Macromolécules Végétales, CNRS (affiliated with Université Joseph Fourier), BP 53, 38041 Grenoble cedex 9, France
3 Institute of Chemical Technology, Technická 5, 166 28 Prague, Czech Republic
1-3 linked Gal or GalNAc sugar residue is the common structure found in several oligosaccharide antigens such as the blood groups A and B, the xeno-antigen, the Forssman antigen and the iGb3 glycolipid. The enzymes involved in the addition of this residue display strong amino acid sequence similarities, suggesting a common fold. From a recently solved crystal structure of the bovine 3-galactosyltransferase complexed with UDP, homology modeling methods were used to build the four other enzymes of this family in their locked conformation. Nucleotide-sugars, Mn2+ ion and oligosaccharide acceptors were docked in the models. Nine different amino acids regions are involved in the substrate binding sites. After geometry optimization of the complexes and analysis of the predicted structures, the basis of the specificities can be rationalized. In the nucleotide-sugar binding site, the specificity between Gal or GalNAc-transferase activity is due to the relative size of two clue amino acids. In the acceptor site, the presence of up to three tryptophan residues define the complexity of the oligosaccharide that can be specifically recognized. The modeling study help in rationalizing the crystallographic data obtained in this family and provide insights on the basis of substrate and donor recognition.
Keywords: Glycosyltransferase, galactosyltransferase, blood group antigens, molecular modeling
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