Insights into the geometrical features underlying beta-O-GIcNAc glycosylation: Water pockets drastically modulate the interactions between the carbohydrate and the peptide backbone

  1. Fernández-Tejada, A. 3
  2. Corzana, F. 3
  3. Busto, J.H. 3
  4. Jiménez-Osés, G. 2
  5. Jiménez-Barbero, J. 1
  6. Avenoza, A. 3
  7. Peregrina, J.M. 3
  1. 1 Centro de Investigaciones Biológicas
    info

    Centro de Investigaciones Biológicas

    Madrid, España

    ROR https://ror.org/04advdf21

  2. 2 Instituto de Nanociencia y Materiales de Aragón
    info

    Instituto de Nanociencia y Materiales de Aragón

    Zaragoza, España

    ROR https://ror.org/031n2c920

  3. 3 Universidad de La Rioja
    info

    Universidad de La Rioja

    Logroño, España

    ROR https://ror.org/0553yr311

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Revista:
Chemistry - A European Journal

ISSN: 0947-6539

Año de publicación: 2009

Volumen: 15

Número: 30

Páginas: 7297-7301

Tipo: Artículo

DOI: 10.1002/CHEM.200901204 PMID: 19544521 SCOPUS: 2-s2.0-67651033651 WoS: WOS:000268621300006 GOOGLE SCHOLAR

Otras publicaciones en: Chemistry - A European Journal

Objetivos de desarrollo sostenible

Resumen

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.