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Titolo:
THE SOLUTION NMR STRUCTURE OF GLUCOSYLATED N-GLYCANS INVOLVED IN THE EARLY STAGES OF GLYCOPROTEIN-BIOSYNTHESIS AND FOLDING
Autore:
PETRESCU AJ; BUTTERS TD; REINKENSMEIER G; PETRESCU S; PLATT FM; DWEK RA; WORMALD MR;
Indirizzi:
UNIV OXFORD,DEPT BIOCHEM,OXFORD GLYCOBIOL INST,S PARKS RD OXFORD OX1 3QU ENGLAND UNIV OXFORD,DEPT BIOCHEM,OXFORD GLYCOBIOL INST OXFORD OX1 3QU ENGLAND
Titolo Testata:
EMBO journal
fascicolo: 14, volume: 16, anno: 1997,
pagine: 4302 - 4310
SICI:
0261-4189(1997)16:14<4302:TSNSOG>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
HISTOCOMPATIBILITY COMPLEX-MOLECULES; ENDOPLASMIC-RETICULUM; LINKED OLIGOSACCHARIDES; GLUCOSIDASE-II; CALNEXIN; GLYCOSYLATION; CONFORMATION; ASSOCIATION; MICROSOMES; CHAPERONE;
Keywords:
GLUCOSYLATED GLYCANS; NMR; OLIGOSACCHARIDE STRUCTURE; PROTEIN FOLDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
39
Recensione:
Indirizzi per estratti:
Citazione:
A.J. Petrescu et al., "THE SOLUTION NMR STRUCTURE OF GLUCOSYLATED N-GLYCANS INVOLVED IN THE EARLY STAGES OF GLYCOPROTEIN-BIOSYNTHESIS AND FOLDING", EMBO journal, 16(14), 1997, pp. 4302-4310

Abstract

Glucosylated oligomannose N-linked oligosaccharides (Glc(x)Man(9)GlcNAc(2) where x = 1-3) are not normally found on mature glycoproteins but are involved in the early stages of glycoprotein biosynthesis and folding as (i) recognition elements during protein N-glycosylation and chaperone recognition and (ii) substrates in the initial steps of N-glycan processing, By inhibiting the first steps of glycan processing in CHO cells using the alpha-glucosidase inhibitor N-butyl-deoxynojirimycin, we have produced sufficient Glc(3)Man(7)GlcNAc(2) for structural analysis by nuclear magnetic resonance (NMR) spectroscopy, Our results show the glucosyl cap to have a single, well-defined conformation independent of the rest of the saccharide. Comparison with the conformation of Man(9)GlcNAc(2), previously determined by NMR and molecular dynamics, shows the mannose residues to be largely unaffected by the presence of the glucosyl cap, Sequential enzymatic cleavage of the glucose residues does not affect the conformation of the remaining saccharide, Modelling of the Glc(3) Man(9)GlcNAc(2), Glc(2)Man(9)GlcNAc(2) and Glc(1)Man(9) GlcNAc(2) conformations shows the glucose residues to be fully accessible for recognition, A more detailed analysis of the conformations allows potential recognition epitopes on the glycans to be identified and can form the basis for understanding the specificity of theglucosidases and chaperones (such as calnexin) that recognize these glycans, with implications for their mechanisms of action.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/09/20 alle ore 11:11:26