For the A2A adenosine receptor (A2AAR), a class A G-protein-coupled receptor (GPCR), reconstituted in n-dodecyl-β-D-maltoside (DDM)/â??â??â??â??â??cholesteryl hemisuccinate (CHS) mixed micelles, previous 19F-NMR studies revealed the presence of multiple simultaneously populated conformational states. Here, we study the influence of a different detergent, lauryl maltose neopentyl glycol (LMNG) in mixed micelles with CHS, and of lipid bilayer nanodiscs on these conformational equilibria. The populations of locally different substates are pronouncedly different in DDM/â??â??â??â??â??CHS and LMNG/â??â??â??â??â??CHS micelles, whereas the A2AAR conformational manifold in LMNG/â??â??â??â??â??CHS micelles is closely similar to that in the lipid bilayer nanodiscs. Considering that nanodiscs represent a closer match of the natural lipid bilayer membrane, these observations support that LMNG/â??â??â??â??â??CHS micelles are a good choice for reconstitution trials of class A GPCRs for NMR studies in solution.
[ASAP] Adenosine A2A Receptor (A2AAR) Ligand Screening Using the 19F-NMR Probe FPPA
Adenosine A2A Receptor (A2AAR) Ligand Screening Using the 19F-NMR Probe FPPA
Jinfeng Zhang, Dandan Feng, Jianjun Cheng, and Kurt Wu?thrich
https://pubs.acs.org/cms/10.1021/jacs.3c04218/asset/images/medium/ja3c04218_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.3c04218
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[NMR paper] Adenosine A2A Receptor (A2AAR) Ligand Screening Using the 19F-NMR Probe FPPA
Adenosine A2A Receptor (A2AAR) Ligand Screening Using the 19F-NMR Probe FPPA
The binding affinity of G protein-coupled receptor (GPCR) ligands is customarily measured by radio-ligand competition experiments. As an alternative approach, ^(19)F nuclear magnetic resonance spectroscopy (^(19)F-NMR) is used for the screening of small-molecule lead compounds in drug discovery; the two methods are complementary in that the measurements are performed with widely different experimental conditions. Here, we used the structure of the A(2A) adenosine receptor (A(2A)AR) complex with...
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[NMR paper] Activation of adenosine A2A receptor by lipids from docosahexaenoic acid revealed by NMR.
Activation of adenosine A2A receptor by lipids from docosahexaenoic acid revealed by NMR.
Related Articles Activation of adenosine A2A receptor by lipids from docosahexaenoic acid revealed by NMR.
Sci Adv. 2020 Mar;6(12):eaay8544
Authors: Mizumura T, Kondo K, Kurita M, Kofuku Y, Natsume M, Imai S, Shiraishi Y, Ueda T, Shimada I
Abstract
The lipid composition of the plasma membrane is a key parameter in controlling signal transduction through G protein-coupled receptors (GPCRs). Adenosine A2A receptor (A2AAR) is located in the...
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03-25-2020 10:28 PM
[NMR paper] Reconstitution and NMR Characterization of the Ion-Channel Accessory Subunit Barttin in Detergents and Lipid-Bilayer Nanodiscs.
Reconstitution and NMR Characterization of the Ion-Channel Accessory Subunit Barttin in Detergents and Lipid-Bilayer Nanodiscs.
Related Articles Reconstitution and NMR Characterization of the Ion-Channel Accessory Subunit Barttin in Detergents and Lipid-Bilayer Nanodiscs.
Front Mol Biosci. 2019;6:13
Authors: Viennet T, Bungert-Plümke S, Elter S, Viegas A, Fahlke C, Etzkorn M
Abstract
Barttin is an accessory subunit of ClC-K chloride channels expressed in the kidney and the inner ear. Main functions of ClC-K/barttin channels are...
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[ASAP] Extrinsic Tryptophans as NMR Probes of Allosteric Coupling in Membrane Proteins: Application to the A2A Adenosine Receptor
Extrinsic Tryptophans as NMR Probes of Allosteric Coupling in Membrane Proteins: Application to the A2A Adenosine Receptor
Matthew T. Eddy, Zhan-Guo Gao, Philip Mannes, Nilkanth Patel, Kenneth A. Jacobson, Vsevolod Katritch, Raymond C. Stevens, Kurt Wüthrich
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.8b03805/20180620/images/medium/ja-2018-03805n_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.8b03805
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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[NMR paper] Extrinsic Tryptophans as NMR Probes of Allosteric Coupling in Membrane Proteins: Application to the A2A Adenosine Receptor.
Extrinsic Tryptophans as NMR Probes of Allosteric Coupling in Membrane Proteins: Application to the A2A Adenosine Receptor.
Extrinsic Tryptophans as NMR Probes of Allosteric Coupling in Membrane Proteins: Application to the A2A Adenosine Receptor.
J Am Chem Soc. 2018 Jun 06;:
Authors: Eddy MT, Gao ZG, Mannes P, Patel N, Jacobson KA, Katritch V, Stevens RC, Wüthrich K
Abstract
Tryptophan indole 15N-1H signals are well separated in nuclear magnetic resonance (NMR) spectra of proteins. Assignment of the indole 15N-1H signals...
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[NMR paper] Nanodiscs for INPHARMA NMR Characterization of GPCRs: Ligand Binding to the Human A2A Adenosine Receptor.
Nanodiscs for INPHARMA NMR Characterization of GPCRs: Ligand Binding to the Human A2A Adenosine Receptor.
Related Articles Nanodiscs for INPHARMA NMR Characterization of GPCRs: Ligand Binding to the Human A2A Adenosine Receptor.
Angew Chem Int Ed Engl. 2017 Apr 21;:
Authors: Fredriksson K, Lottmann P, Hinz S, Onila I, Shymanets A, Harteneck C, Müller CE, Griesinger C, Exner TE
Abstract
G-protein-coupled-receptors (GPCRs) are of fundamental importance for signal transduction through cell membranes. This makes them important...
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04-22-2017 10:30 PM
[NMR paper] NMR metabolomics for identification of adenosine A1 receptor binding compounds from Boesenbergia rotunda rhizomes extract.
NMR metabolomics for identification of adenosine A1 receptor binding compounds from Boesenbergia rotunda rhizomes extract.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR metabolomics for identification of adenosine A1 receptor binding compounds from Boesenbergia rotunda rhizomes extract.
J Ethnopharmacol. 2013 Oct 28;150(1):95-9
Authors: Yuliana ND, Budijanto S, Verpoorte R, Choi YH
Abstract
ETHNOPHARMACOLOGICAL RELEVANCE:...