Glycobiology Advance Access originally published online on January 22, 2003
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Glycobiology, 2003, Vol. 13, No. 5 377-386
© 2003 Oxford University Press
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), 601 rue de la Chimie, BP 53, 38041 Grenoble Cedex 9, France
3 Institute of Chemical Technology, Technická 5, 166 28 Prague, Czech Republic
Received on November 18, 2002; revised on December 9, 2002; accepted on December 17, 2002
A terminal 
1-3 linked Gal or GalNAc sugar residue is the common structure found in several oligosaccharide antigens, such as blood groups A and B, the xeno-antigen, the Forssman antigen, and the isogloboside 3 (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, the Mn2+ ion, and oligosaccharide acceptors were docked in the models. Nine different amino acid 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 helps in rationalizing the crystallographic data obtained in this family and provides insights on the basis of substrate and donor recognition.
1 To whom correspondence should be addressed; e-mail: imberty{at}cermav.cnrs.fr
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