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Insights into the Geometrical Features Underlying β‐ O ‐GlcNAc Glycosylation: Water Pockets Drastically Modulate the Interactions between the Carbohydrate and the Peptide Backbone
Author(s) -
FernándezTejada Alberto,
Corzana Francisco,
Busto Jesús H.,
JiménezOsés Gonzalo,
JiménezBarbero Jesús,
Avenoza Alberto,
Peregrina Jesús M.
Publication year - 2009
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.200901204
Subject(s) - glycosylation , glycopeptide , chemistry , key (lock) , computational biology , peptide , presentation (obstetrics) , biochemistry , information retrieval , computer science , biology , ecology , medicine , antibiotics , radiology
Water pockets at key sites as well as specific hydrogen bonds modulate sugar–peptide interactions in β‐ N ‐acetyl‐ D ‐glucosamine (β‐ O ‐GlcNAc) glycopeptides (see picture). It is likely that these solvent pockets have important biological implications, providing the required presentation of the GlcNAc moieties to interact with their biological receptors.