Glucosylated oligomannose N-linked oligosaccharides (Glc(x)Man9GlcNAc2 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 Glc3Man7GlcNAc2 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 Man9GlcNAc2, 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 Glc3Man9GlcNAc2, Glc2Man9GlcNAc2 and Glc1Man9GlcNAc2 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 the glucosidases and chaperones (such as calnexin) that recognize these glycans, with implications for their mechanisms of action.
Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly.
Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly.
Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly.
J Struct Funct Genomics. 2011 Sep 9;
Authors: Yang Y, Ramelot TA, Cort JR, Wang H, Ciccosanti C, Jiang M, Janjua H, Acton TB, Xiao R, Everett JK, Montelione GT, Kennedy MA
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NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic.
NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic.
NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic.
Nat Chem Biol. 2011 Jan 23;
Authors: Barb AW, Prestegard JH
The N-glycan at Asn297 of the immunoglobulin G Fc fragment modulates cellular responses of the adaptive immune system. However, the underlying mechanism remains undefined, as existing structural data suggest the glycan does not directly engage cell surface receptors. Here we characterize the dynamics of the glycan termini...
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[NMR paper] NMR conformational studies of micelle-bound orexin-B: a neuropeptide involved in the
NMR conformational studies of micelle-bound orexin-B: a neuropeptide involved in the sleep/awake cycle and feeding regulation.
Related Articles NMR conformational studies of micelle-bound orexin-B: a neuropeptide involved in the sleep/awake cycle and feeding regulation.
J Biomol Struct Dyn. 2003 Dec;21(3):341-51
Authors: Miskolzie M, Lucyk S, Kotovych G
The preferred conformation of orexin-B, an orphan G-protein coupled receptor agonist (the human sequence is RSGPPGLQGRLQRLLQASGNHAAGILTM-NH(2)) has been determined by (1)H and (13)C 2D NMR...
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11-24-2010 09:16 PM
[NMR paper] Detection of conserved N-linked glycans and phase-variable lipooligosaccharides and c
Detection of conserved N-linked glycans and phase-variable lipooligosaccharides and capsules from campylobacter cells by mass spectrometry and high resolution magic angle spinning NMR spectroscopy.
Related Articles Detection of conserved N-linked glycans and phase-variable lipooligosaccharides and capsules from campylobacter cells by mass spectrometry and high resolution magic angle spinning NMR spectroscopy.
J Biol Chem. 2003 Jul 4;278(27):24509-20
Authors: Szymanski CM, Michael FS, Jarrell HC, Li J, Gilbert M, Larocque S, Vinogradov E, Brisson JR
...
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[NMR paper] NMR assignment of human ASC2, a self contained protein interaction domain involved in
NMR assignment of human ASC2, a self contained protein interaction domain involved in apoptosis and inflammation.
Related Articles NMR assignment of human ASC2, a self contained protein interaction domain involved in apoptosis and inflammation.
J Biomol NMR. 2002 Jun;23(2):151-2
Authors: Espejo F, Green M, Preece NE, Assa-Munt N
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[NMR paper] Identification of residues involved in the interaction of Staphylococcus aureus fibro
Identification of residues involved in the interaction of Staphylococcus aureus fibronectin-binding protein with the (4)F1(5)F1 module pair of human fibronectin using heteronuclear NMR spectroscopy.
Related Articles Identification of residues involved in the interaction of Staphylococcus aureus fibronectin-binding protein with the (4)F1(5)F1 module pair of human fibronectin using heteronuclear NMR spectroscopy.
Biochemistry. 2000 Mar 21;39(11):2887-93
Authors: Penkett CJ, Dobson CM, Smith LJ, Bright JR, Pickford AR, Campbell ID, Potts JR
Many...
[NMR paper] The structure of the site on adenovirus early region 1A responsible for binding to TA
The structure of the site on adenovirus early region 1A responsible for binding to TATA-binding protein determined by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles The structure of the site on adenovirus early region 1A responsible for binding to TATA-binding protein determined by NMR spectroscopy.
J Biol Chem. 1999 Feb 5;274(6):3503-12
Authors: Molloy DP, Smith KJ, Milner AE, Gallimore PH, Grand RJ
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The solution NMR structure of glucosylated N-glycans involved in the early stages of
Linear Mode
