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Duclos, S ; Da Silva, P ; Vovelle, F ; Piller, F ; Piller, V

Characterization of the UDP-N-acetylgalactosamine binding domain of bovine polypeptide alpha N-acetylgalactosaminyltransferase T1

Protein Engineering Design & Selection 17 (8) 635-646

par Administrateur - publié le , mis à jour le

Abstract :

UDP-GalNAc:polypeptide alphaN-acetylgalactosaminyltransferases (ppGaNTases) transfer GalNAc from UDP-GalNAc to Ser or Thr. Structural features underlying their enzymatic activity and their specificity are still unidentified. In order to get some insight into the donor substrate recognition, we used a molecular modelling approach on a portion of the catalytic site of the bovine ppGaNTase-T1. Fold recognition methods identified as appropriate templates the bovine alpha1,3galactosyltransferase and the human alpha1,3N-acetylgalactosaminyltransferase. A model of the ppGaNTase-T1 nucleotide-sugar binding site was built into which the UDP-GalNAc and the Mn2+ cation were docked.