Insights into the geometrical features underlying beta-O-GIcNAc glycosylation: Water pockets drastically modulate the interactions between the carbohydrate and the peptide backbone
- Fernández-Tejada, A. 3
- Corzana, F. 3
- Busto, J.H. 3
- Jiménez-Osés, G. 2
- Jiménez-Barbero, J. 1
- Avenoza, A. 3
- Peregrina, J.M. 3
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1
Centro de Investigaciones Biológicas
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2
Instituto de Nanociencia y Materiales de Aragón
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3
Universidad de La Rioja
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ISSN: 0947-6539
Datum der Publikation: 2009
Ausgabe: 15
Nummer: 30
Seiten: 7297-7301
Art: Artikel
Andere Publikationen in: Chemistry - A European Journal
Ziele für nachhaltige Entwicklung
Zusammenfassung
A novel and simple model was proposed to explain the different relative orientation of the peptide backbone and presentation of beta-N-scetyl-D- glucosamine (β-O-GlcNAc)-Thr and Ser moieties. The sugar-peptide interactions were modulated by the specific hydrogen bonds and the existence of water pockets at key sites. NMR experiments of the interactions were recorded on a Bruker Avance 400 spectrometer at 298 K to verify the investigations. MAD-tar simulations were performed with AMBER 6.0 (AMBER94) that was implemented with GLYCAM 04 parameters to accurately simulate the computational behavior of the sugar moiety. NOE-derived distances were included as time-averaged coupling constraints along with the scalar coupling constants J. Final trajectories were run using an exponential decay constant of 16 ns and a simulation length of 16 ns with water molecules.