Stabilization of the T1 fragment of glycophorin AN through interactions with N- and O-linked glycans

NMR studies of the highly and densely glycosylated glycoprotein demonstrate that peptide–carbohydrate interactions at the 13 glycosylation sites induce well defined saccharide conformations and extended peptide backbone structures.

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Nature Structural Biology 1996-03, Vol.3 (3), p.228-232
Hauptverfasser:	Pieper, Jörg, Ott, Karl-Heinz, Meyer, Bernd
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Biochemistry Biological Microscopy Biomedical and Life Sciences Carbohydrate Conformation Carbohydrate Sequence correspondence Glycophorin - chemistry Glycosylation Humans Life Sciences Magnetic Resonance Spectroscopy - methods Membrane Biology Models, Molecular Molecular Sequence Data Oligosaccharides - chemistry Peptide Fragments - chemistry Protein Conformation Protein Structure
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Beschreibung
Zusammenfassung:	NMR studies of the highly and densely glycosylated glycoprotein demonstrate that peptide–carbohydrate interactions at the 13 glycosylation sites induce well defined saccharide conformations and extended peptide backbone structures.
ISSN:	1072-8368 1545-9985
DOI:	10.1038/nsb0396-228