Interactions between glycosyltransferases and 2-deoxy glycosyl derivatives of uridine simulated by molecular docking.
The focus of the present work was to investigate interactions between 2-deoxy sugar derivatives of uridine and active sites of N-acetylglucosaminyltransferase I and beta-1,4-galactosyltransferase I. The ligand-protein interactions were simulated with a docking software (GOLD). The results suggest that the synthesized compounds bind the enzyme by a similar mode as the natural substrate.
Wandzik
Ilona
I
Silesian University of Technology, Faculty of Chemistry, Department of Organic Chemistry, Bioorganic Chemistry and Biotechnology, 4 Krzywoustego St., 44-100 Gliwice, Poland. ilona.wandzik@polsl.pl
D001665:Binding Sites; D003198:Computer Simulation; D005700:Galactosyltransferases / Q000378:metabolism*; D008024:Ligands; D017351:N-Acetylglucosaminyltransferases / Q000378:metabolism*; D011485:Protein Binding; D012984:Software; D013329:Structure-Activity Relationship; D014529:Uridine / Q000031:analogs & derivatives / Q000737:chemistry / Q000378:metabolism*
D008024:Ligands; D005700:Galactosyltransferases; D017351:N-Acetylglucosaminyltransferases; C119701:beta-1,4-galactosyltransferase I; C024850:alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase I; D014529:Uridine