Serine versus Threonine Glycosylation: The Methyl Group Causes a Drastic Alteration on the Carbohydrate Orientation and on the Surrounding Water Shell

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

    Centro de Investigaciones Biológicas

    Madrid, España

    ROR https://ror.org/04advdf21

  2. 2 Universidad de La Rioja
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    Universidad de La Rioja

    Logroño, España

    ROR https://ror.org/0553yr311

  3. 3 Instituto de Química Orgánica General
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    Instituto de Química Orgánica General

    Madrid, España

    ROR https://ror.org/05e0q7s59

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Revista:
Journal of the American Chemical Society

ISSN: 0002-7863

Año de publicación: 2007

Volumen: 129

Número: 30

Páginas: 9458-9467

Tipo: Artículo

DOI: 10.1021/JA072181B PMID: 17616194 SCOPUS: 2-s2.0-34547683219 WoS: WOS:000248281100048 GOOGLE SCHOLAR

Otras publicaciones en: Journal of the American Chemical Society

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Síntesis y análisis conformacional de o-glicoaminoacidos y o-glicopeptidos modelo de interés biológico

2006/00086/001

Resumen

Different behavior has been observed for the ψ torsion angle of the glycosidic linkages of D-GalNAc-Ser and D-GalNAc-Thr motifs, allowing the carbohydrate moiety to adopt a completely different orientation. In addition, the fact that the water pockets found in α-D-GalNAc-Thr differ from those obtained for its serine analogue could be related to the different capability that the two model glycopeptides have to structure the surrounding water. This fact could have important biological inferences (i.e., antifreeze activity). © 2007 American Chemical Society.