[NMR paper] NMR evidence for oligosaccharide release from the dendritic-cell specific intercellular adhesion molecule*3-grabbing non-integrin-related (CLEC4M) carbohydrate recognition domain at low pH.
NMR evidence for oligosaccharide release from the dendritic-cell specific intercellular adhesion molecule*3-grabbing non-integrin-related (CLEC4M) carbohydrate recognition domain at low pH.
Related ArticlesNMR evidence for oligosaccharide release from the dendritic-cell specific intercellular adhesion molecule*3-grabbing non-integrin-related (CLEC4M) carbohydrate recognition domain at low pH.
FEBS J. 2014 Aug;281(16):3739-50
Authors: Probert F, Mitchell DA, Dixon AM
Abstract
Dendritic cell-specific intercellular adhesion molecule*3-grabbing non-integrin-related (DC-SIGNR), also known as liver/lymph node-specific intercellular adhesion molecule*3-grabbing non-integrin, CLEC4M, CD209L, and CD299, is a Ca(2+) -dependent lectin that has been implicated in increasing the infection rates of several viruses, including HIV, but the physiological role of DC-SIGNR in healthy cells is currently not known with certainty. A close homologue of DC-SIGNR, dendritic-cell specific intercellular adhesion molecule*3-grabbing non-integrin, has been shown to act as a recycling endocytic receptor, which binds pathogens at the cell's surface and then releases them in the low pH environment of endosomal compartments. However, it is currently under debate in the literature as to whether DC-SIGNR plays a similar role. In this work, we used NMR to explore whether the DC-SIGNR carbohydrate recognition domain (CRD) shows any pH dependence in its ability to bind carbohydrates and Ca(2+) . We found clear evidence of reduced or abolished CRD-binding affinities for three different glycans at low pH (4.2) as compared to neutral pH (6.8). We also report the assignment of the DC-SIGNR CRD in the apo form, and use these new results to characterize the degree of structural rearrangement upon binding (or release) of Ca(2+) . Finally, we report a differential effect of pH on the affinities of glycans containing mannose exclusively versus glycans containing GlcNAc moieties. Our results lead us to propose that the DC-SIGNR CRD rapidly and reversibly releases glycan ligands and Ca(2+) at reduced pH (behaviour that would be expected for an endocytic receptor), and that the binding of mannose-containing oligosaccharides is more strongly affected by pH than the binding of GlcNAc-containing oligosaccharides.
[NMR paper] In-cell NMR: an emerging approach for monitoring metal-related events in living cells.
In-cell NMR: an emerging approach for monitoring metal-related events in living cells.
Related Articles In-cell NMR: an emerging approach for monitoring metal-related events in living cells.
Metallomics. 2013 Nov 8;
Authors: Li H, Sun H
Abstract
In-cell NMR, an isotope-assisted multi-dimensional NMR technique, has been proven to be successful in the investigation of protein dynamics, folding, conformational changes induced by binding events, posttranslational modification in the complex native environments, as well as in vivo drug...
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[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] Protein-Carbohydrate Interactions Studied by NMR. from Molecular Recognition to Drug Design.
Protein-Carbohydrate Interactions Studied by NMR. from Molecular Recognition to Drug Design.
Related Articles Protein-Carbohydrate Interactions Studied by NMR. from Molecular Recognition to Drug Design.
Curr Protein Pept Sci. 2012 Dec 10;
Authors: Fernandez-Alonso MD, Diaz D, Berbis MA, Marcelo F, Jimenez-Barbero J
Abstract
Diseases that result from infection are, in general, a consequence of specific interactions between a pathogenic organism and the cells. The study of host-pathogen interactions has provided insights for the design of...
[NMR paper] Solution structure of the peptidoglycan binding domain of Bacillus subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-related repeats by NMR.
Solution structure of the peptidoglycan binding domain of Bacillus subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-related repeats by NMR.
Related Articles Solution structure of the peptidoglycan binding domain of Bacillus subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-related repeats by NMR.
Biochemistry. 2005 Aug 2;44(30):10153-63
Authors: Mishima M, Shida T, Yabuki K, Kato K, Sekiguchi J, Kojima C
Bacillus subtilis CwlC is a cell wall lytic N-acetylmuramoyl-l-alanine amidase that plays an...
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[NMR paper] 1H NMR assignment and secondary structure of the cell adhesion type III module of fib
1H NMR assignment and secondary structure of the cell adhesion type III module of fibronectin.
Related Articles 1H NMR assignment and secondary structure of the cell adhesion type III module of fibronectin.
Biochemistry. 1992 Feb 25;31(7):2068-73
Authors: Baron M, Main AL, Driscoll PC, Mardon HJ, Boyd J, Campbell ID
The secondary structure of the tenth type III module from human fibronectin has been determined using NMR. This type of module appears many times in a wide variety of proteins. The type III module described here contains an...
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[NMR paper] Cell adhesion promoting peptide GVKGDKGNPGWPGAP from the collagen type IV triple heli
Cell adhesion promoting peptide GVKGDKGNPGWPGAP from the collagen type IV triple helix: cis/trans proline-induced multiple 1H NMR conformations and evidence for a KG/PG multiple turn repeat motif in the all-trans proline state.
Related Articles Cell adhesion promoting peptide GVKGDKGNPGWPGAP from the collagen type IV triple helix: cis/trans proline-induced multiple 1H NMR conformations and evidence for a KG/PG multiple turn repeat motif in the all-trans proline state.
Biochemistry. 1991 Aug 20;30(33):8251-67
Authors: Mayo KH, Parra-Diaz D, McCarthy JB,...
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[NMR paper] Cell adhesion promoting peptide GVKGDKGNPGWPGAP from the collagen type IV triple heli
Cell adhesion promoting peptide GVKGDKGNPGWPGAP from the collagen type IV triple helix: cis/trans proline-induced multiple 1H NMR conformations and evidence for a KG/PG multiple turn repeat motif in the all-trans proline state.
Related Articles Cell adhesion promoting peptide GVKGDKGNPGWPGAP from the collagen type IV triple helix: cis/trans proline-induced multiple 1H NMR conformations and evidence for a KG/PG multiple turn repeat motif in the all-trans proline state.
Biochemistry. 1991 Aug 20;30(33):8251-67
Authors: Mayo KH, Parra-Diaz D, McCarthy JB,...
NMR evidence for oligosaccharide release from the dendritic-cell specific intercellular adhesion molecule*3-grabbing non-integrin-related (CLEC4M) carbohydrate recognition domain at low pH.
Linear Mode
