By nature of conducting ions, transporting substrates and transducing signals, membrane channels, transporters and receptors are expected to exhibit intrinsic conformational dynamics. It is therefore of great interest and importance to understand the various properties of conformational dynamics acquired by these proteins, for example, the relative population of states, exchange rate, conformations of multiple states, and how small molecule ligands modulate the conformational exchange. Because small molecule binding to membrane proteins can be weak and/or dynamic, structural characterization of these effects is very challenging. This review describes several NMR studies of membrane protein dynamics, ligand-induced conformational rearrangements, and the effect of ligand binding on the equilibrium of conformational exchange. The functional significance of the observed phenomena is discussed.
[NMR paper] A Functional NMR for Membrane Proteins: Dynamics, Ligand Binding, and Allosteric Modulation.
A Functional NMR for Membrane Proteins: Dynamics, Ligand Binding, and Allosteric Modulation.
A Functional NMR for Membrane Proteins: Dynamics, Ligand Binding, and Allosteric Modulation.
Protein Sci. 2016 Mar 1;
Authors: Oxenoid K, Chou JJ
Abstract
By nature of conducting ions, transporting substrates and transducing signals, membrane channels, transporters and receptors are expected to exhibit intrinsic conformational dynamics. It is therefore of great interest and importance to understand the various properties of...
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03-02-2016 07:20 PM
A Functional NMR for Membrane Proteins: Dynamics, Ligand Binding, and Allosteric Modulation
A Functional NMR for Membrane Proteins: Dynamics, Ligand Binding, and Allosteric Modulation
SUMMARY
By nature of conducting ions, transporting substrates and transducing signals, membrane channels, transporters and receptors are expected to exhibit intrinsic conformational dynamics. It is therefore of great interest and importance to understand the various properties of conformational dynamics acquired by these proteins, e.g., the relative population of states, exchange rate, conformations of multiple states, and how small molecule ligands modulate the conformational exchange. Because...
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03-01-2016 05:59 PM
[NMR paper] Identification of the binding site of an allosteric ligand using STD-NMR, docking, and CORCEMA-ST calculations.
Identification of the binding site of an allosteric ligand using STD-NMR, docking, and CORCEMA-ST calculations.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary_FullTextOnline_120x27.gif http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary_FullTextOnline_120x27.gif http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc-MS.gif Related Articles Identification of the binding...
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10-27-2015 12:33 PM
[NMR paper] Functional dynamics of cell surface membrane proteins
Functional dynamics of cell surface membrane proteins
Publication date: Available online 22 November 2013
Source:Journal of Magnetic Resonance</br>
Author(s): Noritaka Nishida , Masanori Osawa , Koh Takeuchi , Shunsuke Imai , Pavlos Stampoulis , Yutaka Kofuku , Takumi Ueda , Ichio Shimada</br>
Cell surface receptors are integral membrane proteins that receive external stimuli, and transmit signals across plasma membranes. In the conventional view of receptor activation, ligand binding to the extracellular side of the receptor induces conformational changes,...
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11-23-2013 04:05 AM
[NMR paper] Unique Structure and Dynamics of the EphA5 Ligand Binding Domain Mediate Its Binding Specificity as Revealed by X-ray Crystallography, NMR and MD Simulations.
Unique Structure and Dynamics of the EphA5 Ligand Binding Domain Mediate Its Binding Specificity as Revealed by X-ray Crystallography, NMR and MD Simulations.
Unique Structure and Dynamics of the EphA5 Ligand Binding Domain Mediate Its Binding Specificity as Revealed by X-ray Crystallography, NMR and MD Simulations.
PLoS One. 2013;8(9):e74040
Authors: Huan X, Shi J, Lim L, Mitra S, Zhu W, Qin H, Pasquale EB, Song J
Abstract
The 16 EphA and EphB receptors represent the largest family of receptor tyrosine kinases, and their interactions...
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10-03-2013 03:31 PM
Functional dynamics of proteins revealed by solution NMR
Functional dynamics of proteins revealed by solution NMR
October 2012
Publication year: 2012
Source:Current Opinion in Structural Biology, Volume 22, Issue 5</br>
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Solution NMR spectroscopy can analyze the dynamics of proteins on a wide range of timescales, from picoseconds to even days, in a site-specific manner, and thus its results are complementary to the detailed but largely static structural information obtained by X-ray crystallography. We review recent progresses in a variety of NMR techniques, including relaxation dispersion and paramagnetic relaxation...
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02-03-2013 10:13 AM
Solid-state 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin [Biophysics and Computational Biology]
Solid-state 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin
Struts, A. V., Salgado, G. F. J., Brown, M. F....
Date: 2011-05-17
Rhodopsin is a canonical member of the family of G protein-coupled receptors, which transmit signals across cellular membranes and are linked to many drug interventions in humans. Here we show that solid-state 2H NMR relaxation allows investigation of light-induced changes in local ps–ns time scale motions of retinal bound to rhodopsin. Site-specific 2H labels were introduced into methyl groups of the...
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05-17-2011 08:40 PM
Solid-state 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin.
Solid-state 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin.
Solid-state 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin.
Proc Natl Acad Sci U S A. 2011 Apr 28;
Authors: Struts AV, Salgado GF, Brown MF
Rhodopsin is a canonical member of the family of G protein-coupled receptors, which transmit signals across cellular membranes and are linked to many drug interventions in humans. Here we show that solid-state (2)H NMR relaxation...
A functional NMR for membrane proteins: dynamics, ligand binding, and allosteric modulation
Linear Mode
