Related ArticlesThe role of NMR spectroscopy in mapping the conformational landscape of GPCRs.
Curr Opin Struct Biol. 2019 May 07;57:145-156
Authors: Bostock MJ, Solt AS, Nietlispach D
Abstract
Over recent years, nuclear magnetic resonance (NMR) spectroscopy has developed into a powerful mechanistic tool for the investigation of G protein-coupled receptors (GPCRs). NMR provides insights which underpin the dynamic nature of these important receptors and reveals experimental evidence for a complex conformational energy landscape that is explored during receptor activation resulting in signalling. NMR studies have highlighted both the dynamic properties of different receptor states as well as the exchange pathways and intermediates formed during activation, extending the static view of GPCRs obtained from other techniques. NMR studies can be undertaken in realistic membrane-like phospholipid environments and an ever-increasing choice of labelling strategies provides comprehensive, receptor-wide information. Combined with other structural methods, NMR is contributing to our understanding of allosteric signal propagation and the interaction of GPCRs with intracellular binding partners (IBP), crucial to explaining cellular signalling.
PMID: 31075520 [PubMed - as supplied by publisher]
[ASAP] Illuminating the Energy Landscape of GPCRs: The Key Contribution of Solution-State NMR Associated with Escherichia coli as an Expression Host
Illuminating the Energy Landscape of GPCRs: The Key Contribution of Solution-State NMR Associated with Escherichia coli as an Expression Host
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00035/20180412/images/medium/bi-2018-00035s_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00035
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04-13-2018 01:15 AM
[NMR paper] Illuminating the energy landscape of GPCRs: the key contribution of solution-state NMR associated with Escherichia coli as an expression host.
Illuminating the energy landscape of GPCRs: the key contribution of solution-state NMR associated with Escherichia coli as an expression host.
Related Articles Illuminating the energy landscape of GPCRs: the key contribution of solution-state NMR associated with Escherichia coli as an expression host.
Biochemistry. 2018 Apr 02;:
Authors: Casiraghi M, Damian M, Lescop E, Baneres JL, Catoire LJ
Abstract
Conformational dynamics of GPCRs are central to their function but are difficult to explore at the atomic scale. Solution-state...
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04-03-2018 08:27 PM
[NMR paper] Unraveling the conformational landscape of ligand binding to Glucose/Galactose-binding protein by paramagnetic NMR and MD simulations.
Unraveling the conformational landscape of ligand binding to Glucose/Galactose-binding protein by paramagnetic NMR and MD simulations.
Related Articles Unraveling the conformational landscape of ligand binding to Glucose/Galactose-binding protein by paramagnetic NMR and MD simulations.
ACS Chem Biol. 2016 May 24;
Authors: Unione L, Ortega G, Mallagaray A, Corzana F, Perez-Castells J, Canales A, Jimenez-Barbero J, Millet O
Abstract
Protein dynamics related to function can be nowadays structurally well characterized (i. e....
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05-25-2016 02:33 PM
[NMR paper] Nuts and Bolts of CF3 and CH 3 NMR Toward the Understanding of Conformational Exchange of GPCRs.
Nuts and Bolts of CF3 and CH 3 NMR Toward the Understanding of Conformational Exchange of GPCRs.
Related Articles Nuts and Bolts of CF3 and CH 3 NMR Toward the Understanding of Conformational Exchange of GPCRs.
Methods Mol Biol. 2015;1335:39-51
Authors: Prosser RS, Kim TH
Abstract
With the advent of efficient protein expression and functional purification protocols, it is now possible to reconstitute many G protein-coupled receptors (GPCRs) in detergent micelles at concentrations of 25 ?M or more. Such concentrations are...
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08-12-2015 10:04 PM
[NMR paper] Mapping Protein Conformational Energy Landscapes Using NMR and Molecular Simulation.
Mapping Protein Conformational Energy Landscapes Using NMR and Molecular Simulation.
Mapping Protein Conformational Energy Landscapes Using NMR and Molecular Simulation.
Chemphyschem. 2013 May 23;
Authors: Guerry P, Mollica L, Blackledge M
Abstract
Nuclear magnetic resonance (NMR) spectroscopy provides detailed understanding of the nature and extent of protein dynamics on physiologically important timescales. We present recent advances in the combination of NMR with state-of-the-art molecular simulation that are providing unique new...
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05-25-2013 12:05 PM
Mapping the Landscape of RNA Dynamics with NMR Spectroscopy.
Mapping the Landscape of RNA Dynamics with NMR Spectroscopy.
Mapping the Landscape of RNA Dynamics with NMR Spectroscopy.
Acc Chem Res. 2011 Sep 6;
Authors: Rinnenthal J, Buck J, Ferner J, Wacker A, Fu?rtig B, Schwalbe H
Abstract
Among the three major classes of biomacromolecules (DNA, RNA, and proteins) RNA's pronounced dynamics are the most explicitly linked to its wide variety of functions, which include catalysis and the regulation of transcription, translation, and splicing. These functions are mediated by a range of RNA...
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[NMR paper] NMR relaxation studies of the role of conformational entropy in protein stability and
NMR relaxation studies of the role of conformational entropy in protein stability and ligand binding.
Related Articles NMR relaxation studies of the role of conformational entropy in protein stability and ligand binding.
Acc Chem Res. 2001 May;34(5):379-88
Authors: Stone MJ
Recent advances in the measurement and analysis of protein NMR relaxation data have made it possible to characterize the dynamical properties of many backbone and side chain groups. With certain caveats, changes in flexibility that occur upon ligand binding, mutation, or...
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11-19-2010 08:32 PM
[NMR paper] Mapping the nucleotide-dependent conformational change of human N-ras p21 in solution
Mapping the nucleotide-dependent conformational change of human N-ras p21 in solution by heteronuclear-edited proton-observed NMR methods.
Related Articles Mapping the nucleotide-dependent conformational change of human N-ras p21 in solution by heteronuclear-edited proton-observed NMR methods.
Biochemistry. 1993 Jul 6;32(26):6763-72
Authors: Hu JS, Redfield AG
Heteronuclear-edited proton-detected NMR methods are used to study the nucleotide-dependent conformational change between GDP- and GTP gamma S-bound forms of human N-ras p21. Amide...
The role of NMR spectroscopy in mapping the conformational landscape of GPCRs.
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