[Molecular modelling of glycans: three-dimensional structure and protein fraction interaction. The example of rabbit sero-transferrin].
On the basis of experimental data and of computer calculations using the Tripos 5.3 force field in order to examine the three-dimensional structures which are sterically feasible and the conformations which are energetically the most favourable, we have designed a program of molecular modelling of biantennary glycans of the N-acetyllactosaminic type (complex type). We demonstrate that, in absence of any interaction with the protein, a high number of glycan conformations exists which can be classified into five basic conformations, four of which have already been described. In fact, in addition to the Y-, T-, "bird" and "broken-wing" conformations, a "back-folded wing" conformation is energetically feasible. In contrast, the glycan linked to the protein is immobilized into only one conformation: the "broken-wing" conformation. Forming a bridge between the two lobes of the peptide chain, it probably contributes to the maintenance of the protein in a biologically active conformation.
Mazurier
J
J
Laboratoire de Chimie biologique, U.M.R. n. 111 du C.N.R.S., Université des Sciences, Villeneuve-d'Ascq.
Dauchez
M
M
Vergoten
G
G
Montreuil
J
J
Spik
G
G
D000818:Animals; D015195:Drug Design; D004347:Drug Interactions; D008956:Models, Chemical; D010455:Peptides / Q000494:pharmacology; D011134:Polysaccharides / Q000737:chemistry* / Q000494:pharmacology; D011487:Protein Conformation; D011817:Rabbits; D014168:Transferrin / Q000737:chemistry*
D010455:Peptides; D011134:Polysaccharides; D014168:Transferrin
Modélisation moléculaire des glycannes: structure tridimensionnelle et interaction avec la fraction protéique. L'exemple de la sérotransferrine de lapin.