Yos9 is an essential component of the endoplasmic reticulum associated protein degradation (ERAD) system that is responsible for removing terminally misfolded proteins from the ER lumen and mediating proteasomal degradation in the cytosol. Glycoproteins that fail to attain their native conformation in the ER expose a distinct oligosaccharide structure, a terminal α1,6-linked mannose residue, that is specifically recognized by the mannose 6-phoshate receptor homology (MRH) domain of Yos9. We have determined the structure of the MRH domain of Yos9 in its free form and complexed with 3α, 6α-mannopentaose. We show that binding is achieved by loops between β-strands performing an inward movement and that this movement also affects the entire β-barrel leading to a twist. These rearrangements may facilitate the processing of client proteins by downstream acting factors. In contrast, other oligosaccharides such as 2α-mannobiose bind weakly with only locally occurring chemical shift changes underscoring the specificity of this substrate selection process within ERAD.
Fluorine pharma: Quality control by NMR
Fluorine pharma: Quality control by NMR
http://www.spectroscopynow.com/common/images/thumbnails/1600c98c38f.jpgRoutine analysis and quality control of fluorine-containing pharmaceuticals could now be possible with the application of the relatively simple and straightforward technique of fluorine-19 nuclear magnetic resonance (NMR) spectroscopy, according to researchers in Kenya and Germany.
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12-01-2017 08:23 AM
[NMR paper] Breaking the limits in analyzing carbohydrate recognition by NMR: Resolving Branch-Selective Interaction of a Tetraantennary N-Glycan with lectins
Breaking the limits in analyzing carbohydrate recognition by NMR: Resolving Branch-Selective Interaction of a Tetraantennary N-Glycan with lectins
Abstract: The biological recognition of complex-type N-glycans is part of many key physiological and pathological events. Despite their importance, the structural characterization of these events remains an unsolved task. The inherent flexibility of N-glycans hampers crystallization and the chemical equivalence of individual branches precludes their NMR characterization. By using a chemoenzymatically synthesized tetraantennary N-glycan...
Low-Field Permanent Magnets for Industrial Process and Quality Control
Low-Field Permanent Magnets for Industrial Process and Quality Control
Publication date: Available online 30 September 2013
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): J. Mitchell , L.F. Gladden , T.C. Chandrasekera , E.J. Fordham</br>
In this review we focus on the technology associated with lowfield NMR. We present the current state-of-the-art in low-field NMR hardware and experiments, considering general magnet designs, rf performance, data processing and interpretation. We provide guidance on obtaining the optimum results from...
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09-30-2013 03:48 PM
[NMR paper] Solution NMR analyses of the C-type carbohydrate recognition domain of DC-SIGNR reveal different binding modes for HIV-derived oligosaccharides and smaller glycan fragments.
Solution NMR analyses of the C-type carbohydrate recognition domain of DC-SIGNR reveal different binding modes for HIV-derived oligosaccharides and smaller glycan fragments.
Related Articles Solution NMR analyses of the C-type carbohydrate recognition domain of DC-SIGNR reveal different binding modes for HIV-derived oligosaccharides and smaller glycan fragments.
J Biol Chem. 2013 Jun 20;
Authors: Probert F, Whittaker SB, Crispin M, Mitchell DA, Dixon AM
Abstract
The C-type lectin DC-SIGNR (Dendritic Cell-Specific ICAM-3-Grabbing...
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06-25-2013 12:17 AM
[NMR paper] Fluorinated Carbohydrates as Lectin Ligands: Dissecting Glycan-Cyanovirin Interactions by Using 19 F NMR Spectroscopy.
Fluorinated Carbohydrates as Lectin Ligands: Dissecting Glycan-Cyanovirin Interactions by Using 19 F NMR Spectroscopy.
Fluorinated Carbohydrates as Lectin Ligands: Dissecting Glycan-Cyanovirin Interactions by Using 19 F NMR Spectroscopy.
Chemistry. 2013 Feb 28;
Authors: Matei E, André S, Glinschert A, Infantino AS, Oscarson S, Gabius HJ, Gronenborn AM
Abstract
NMR spectroscopy and isothermal titration calorimetry (ITC) are powerful methods to investigate ligand-protein interactions. Here, we present a versatile and sensitive fluorine NMR...
Structural investigation of glycan recognition by the ERAD quality control lectin Yos9
Linear Mode
