Serine versus threonine glycosylation: the methyl group causes a drastic alteration on the carbohydrate orientation and on the surrounding water shell.
Different behavior has been observed for the psi 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 alpha-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).
Corzana
Francisco
F
Departamento de Química, Universidad de La Rioja, UA-CSIC, Madre de Dios 51, Logroño, Spain.
Busto
Jesús H
JH
Jiménez-Osés
Gonzalo
G
García de Luis
Marisa
M
Asensio
Juan L
JL
Jiménez-Barbero
Jesús
J
Peregrina
Jesús M
JM
Avenoza
Alberto
A
D002241:Carbohydrates / Q000737:chemistry; D006020:Glycopeptides / Q000737:chemistry*; D006031:Glycosylation; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011506:Proteins / Q000737:chemistry*; D012694:Serine / Q000737:chemistry*; D013499:Surface Properties; D013912:Threonine / Q000737:chemistry*; D014867:Water / Q000737:chemistry*
D002241:Carbohydrates; D006020:Glycopeptides; D011506:Proteins; D014867:Water; D013912:Threonine; D012694:Serine