Significance G protein-coupled receptor (GPCR) structures determined by X-ray crystallography or cryo-electron microscopy include 28 receptors for which complexes with agonists and antagonists can be compared. In all these comparisons, an interatomic distance representing the size of the orthosteric ligand binding groove differs by less than 2.9 Å. In this report, ^(19)F-NMR observations of the NK1R-bound drug molecule aprepitant show that the orthosteric binding groove undergoes transient...
[NMR paper] Rapid (2)H NMR Transverse Relaxation of Perdeuterated Lipid Acyl Chains of Membrane with Bound Viral Fusion Peptide Supports Large-Amplitude Motions of These Chains That Can Catalyze Membrane Fusion
Rapid (2)H NMR Transverse Relaxation of Perdeuterated Lipid Acyl Chains of Membrane with Bound Viral Fusion Peptide Supports Large-Amplitude Motions of These Chains That Can Catalyze Membrane Fusion
An early step in cellular infection by a membrane-enveloped virus like HIV or influenza is joining (fusion) of the viral and cell membranes. Fusion is catalyzed by a viral protein that typically includes an apolar "fusion peptide" (fp) segment that binds the target membrane prior to fusion. In this study, the effects of nonhomologous HIV and influenza fp's on lipid acyl chain motion are probed...
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[NMR paper] Human substance P receptor binding mode of the antagonist drug aprepitant by NMR and crystallography.
Human substance P receptor binding mode of the antagonist drug aprepitant by NMR and crystallography.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_npg.gif 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 Human substance P receptor binding mode of the antagonist drug aprepitant by NMR and crystallography.
Nat Commun. 2019 02 07;10(1):638
Authors: Chen S, Lu M, Liu D, Yang L, Yi C, Ma L, Zhang H, Liu Q,...
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GPCR's Internal Dynamics Probed with NMR - Genetic Engineering & Biotechnology News
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GPCR's Internal Dynamics Probed with NMR
Genetic Engineering & Biotechnology News
These scientists used nuclear magnetic resonance (NMR) spectroscopy to capture many different conformations of a GPCR protein called the A2A adenosine receptor (A2AAR). A2AAR, which regulates blood flow and inflammation and mediates the effects of ...
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GPCR's Internal Dynamics Probed with NMR - Genetic Engineering & Biotechnology News
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[NMR paper] NMR structure and dynamics of the agonist dynorphin peptide bound to the human kappa opioid receptor.
NMR structure and dynamics of the agonist dynorphin peptide bound to the human kappa opioid receptor.
Related Articles NMR structure and dynamics of the agonist dynorphin peptide bound to the human kappa opioid receptor.
Proc Natl Acad Sci U S A. 2015 Sep 8;
Authors: O'Connor C, White KL, Doncescu N, Didenko T, Roth BL, Czaplicki G, Stevens RC, Wüthrich K, Milon A
Abstract
The structure of the dynorphin (1-13) peptide (dynorphin) bound to the human kappa opioid receptor (KOR) has been determined by liquid-state NMR spectroscopy....
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[NMR paper] Structure and Backbone Dynamics of vanadate-bound PRL-3: Comparison of 15N NMR Relaxation Profiles of free and vanadate-bound PRL-3.
Structure and Backbone Dynamics of vanadate-bound PRL-3: Comparison of 15N NMR Relaxation Profiles of free and vanadate-bound PRL-3.
Related Articles Structure and Backbone Dynamics of vanadate-bound PRL-3: Comparison of 15N NMR Relaxation Profiles of free and vanadate-bound PRL-3.
Biochemistry. 2014 Jul 1;
Authors: Jeong KW, Kang DI, Lee E, Shin A, Jin B, Park YG, Lee CK, Kim EH, Jeon YH, Kim EE, Kim Y
Abstract
Phosphatases of regenerating liver (PRLs) constitute a novel class of small, prenylated phosphatases with oncogenic...
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[NMR paper] Vanishing amplitude of backbone dynamics causes a true protein dynamical transition: H2 NMR studies on perdeuterated C-phycocyanin.
Vanishing amplitude of backbone dynamics causes a true protein dynamical transition: H2 NMR studies on perdeuterated C-phycocyanin.
Vanishing amplitude of backbone dynamics causes a true protein dynamical transition: H2 NMR studies on perdeuterated C-phycocyanin.
Phys Rev E Stat Nonlin Soft Matter Phys. 2014 Mar;89(3-1):032710
Authors: Kämpf K, Kremmling B, Vogel M
Abstract
Using a combination of H2 nuclear magnetic resonance (NMR) methods, we study internal rotational dynamics of the perdeuterated protein C-phycocyanin...
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[NMR paper] NMR structure of a receptor-bound G-protein peptide.
NMR structure of a receptor-bound G-protein peptide.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_nature.gif Related Articles NMR structure of a receptor-bound G-protein peptide.
Nature. 1993 May 20;363(6426):276-81
Authors: Dratz EA, Furstenau JE, Lambert CG, Thireault DL, Rarick H, Schepers T, Pakhlevaniants S, Hamm HE
Heterotrimeric GTP-binding proteins (G proteins) regulate cellular activity by coupling to hormone or sensory receptors. Stimulated receptors catalyse the release of GDP from G protein...
GPCR large-amplitude dynamics by (19)F-NMR of aprepitant bound to the neurokinin 1 receptor
Linear Mode
