Intrinsically disordered regions (IDRs) are common and important functional domains in many proteins. However, IDRs are difficult to target for drug development due to the lack of defined structures which would facilitate the identification of possible drug-binding pockets. Galectin-3 is a carbohydrate-binding protein of which overexpression has been implicated in a wide variety of disorders including cancer and inflammation. Apart from its carbohydrate recognition/binding domain (CRD),...
[NMR paper] Galectin-Glycan Interactions: Guidelines for Monitoring by 77 Se NMR Spectroscopy, and Solvent (H2 O/D2 O) Impact on Binding.
Galectin-Glycan Interactions: Guidelines for Monitoring by 77 Se NMR Spectroscopy, and Solvent (H2 O/D2 O) Impact on Binding.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7388-69-wiley-full-text.png http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.png Related Articles Galectin-Glycan Interactions: Guidelines for Monitoring by 77 Se NMR Spectroscopy, and Solvent (H2 O/D2 O) Impact on Binding.
Chemistry. 2021 Jan 04;27(1):316-325
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02-18-2021 03:17 PM
A CON-based NMR assignment strategy for pro-rich intrinsically disordered proteins with low signal dispersion: the C-terminal domain of histone H1.0 as a case study
A CON-based NMR assignment strategy for pro-rich intrinsically disordered proteins with low signal dispersion: the C-terminal domain of histone H1.0 as a case study
Abstract
The C-terminal domain of histone H1.0 (C-H1.0) is involved in DNA binding and is a main determinant of the chromatin condensing properties of histone H1.0. Phosphorylation at the (S/T)-P-X-(K/R) motifs affects DNA binding and is crucial for regulation of C-H1.0 function. Since C-H1.0 is an intrinsically disordered domain, solution NMR is an excellent approach to characterize the...
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11-25-2018 06:02 AM
[NMR paper] Chemical Shifts of the Carbohydrate Binding Domain of Galectin-3 from Magic Angle Spinning NMR and Hybrid Quantum Mechanics/Molecular Mechanics Calculations.
Chemical Shifts of the Carbohydrate Binding Domain of Galectin-3 from Magic Angle Spinning NMR and Hybrid Quantum Mechanics/Molecular Mechanics Calculations.
Chemical Shifts of the Carbohydrate Binding Domain of Galectin-3 from Magic Angle Spinning NMR and Hybrid Quantum Mechanics/Molecular Mechanics Calculations.
J Phys Chem B. 2018 Mar 02;:
Authors: Kraus J, Gupta R, Lu M, Yehl JB, Case DA, Gronenborn AM, Akke M, Polenova T
Abstract
Magic angle spinning NMR spectroscopy is uniquely suited to probe the structure and dynamics of...
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03-03-2018 12:01 PM
[NMR paper] Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment.
Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment.
Related Articles Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment.
BMB Rep. 2016 Apr 4;
Authors: Tompa P, Kim KH, Bokor M, Kamasa P, Tantos Á, Fritz B, Kim DH, Lee C, Verebélyi T, Tompa K
Abstract
Wide-line 1H NMR intensity and differential scanning calorimetry measurements were carried out on the intrinsically disordered...
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07-16-2016 10:22 PM
[NMR paper] NMR assignments of the C-terminal domain of human galectin-8.
NMR assignments of the C-terminal domain of human galectin-8.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR assignments of the C-terminal domain of human galectin-8.
Biomol NMR Assign. 2015 Oct;9(2):427-30
Authors: Liu CH, Chien CT, Lin CH, Hsu ST
Abstract
Galectins recognize ?-galectosides to promote a variety of cellular functions. Despite their sequence variations, all galectins share the same carbohydrate recognition...
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06-21-2016 01:30 PM
[NMR paper] Intra- and inter-molecular interactions of human galectin-3: assessment by full-assignment-based NMR.
Intra- and inter-molecular interactions of human galectin-3: assessment by full-assignment-based NMR.
Related Articles Intra- and inter-molecular interactions of human galectin-3: assessment by full-assignment-based NMR.
Glycobiology. 2016 Feb 23;
Authors: Ippel H, Miller MC, Vértesy S, Zhang Y, Cañada FJ, Suylen D, Umemoto K, Romanò C, Hackeng T, Tai G, Leffler H, Kopitz J, André S, Kübler D, Jiménez-Barbero J, Oscarson S, Gabius HJ, Mayo KH
Abstract
Galectin-3 is an adhesion/growth-regulatory protein with a modular design...
Targeting disordered-structured domain interactions in Galectin-3 based on NMR and enhanced MD
Linear Mode
