[NMR paper] NMR characterization of HIV-1 reverse transcriptase binding to various non-nucleoside reverse transcriptase inhibitors with different activities.
Related ArticlesNMR characterization of HIV-1 reverse transcriptase binding to various non-nucleoside reverse transcriptase inhibitors with different activities.
Sci Rep. 2015;5:15806
Authors: Thammaporn R, Yagi-Utsumi M, Yamaguchi T, Boonsri P, Saparpakorn P, Choowongkomon K, Techasakul S, Kato K, Hannongbua S
Abstract
Human immunodeficiency virus type 1 reverse transcriptase (HIV-1 RT) is an important target for antiviral therapy against acquired immunodeficiency syndrome. However, the efficiency of available drugs is impaired most typically by drug-resistance mutations in this enzyme. In this study, we applied a nuclear magnetic resonance (NMR) spectroscopic technique to the characterization of the binding of HIV-1 RT to various non-nucleoside reverse transcriptase inhibitors (NNRTIs) with different activities, i.e., nevirapine, delavirdine, efavirenz, dapivirine, etravirine, and rilpivirine. (1)H-(13)C heteronuclear single-quantum coherence (HSQC) spectral data of HIV-1 RT, in which the methionine methyl groups of the p66 subunit were selectively labeled with (13)C, were collected in the presence and absence of these NNRTIs. We found that the methyl (13)C chemical shifts of the M230 resonance of HIV-1 RT bound to these drugs exhibited a high correlation with their anti-HIV-1 RT activities. This methionine residue is located in proximity to the NNRTI-binding pocket but not directly involved in drug interactions and serves as a conformational probe, indicating that the open conformation of HIV-1 RT was more populated with NNRTIs with higher inhibitory activities. Thus, the NMR approach offers a useful tool to screen for novel NNRTIs in developing anti-HIV drugs.
[NMR paper] Tripeptides on Gold Nanoparticles: Structural Differences between Two Reverse Sequences as Determined by Solid-State NMR and DFT Calculations.
Tripeptides on Gold Nanoparticles: Structural Differences between Two Reverse Sequences as Determined by Solid-State NMR and DFT Calculations.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Tripeptides on Gold Nanoparticles: Structural Differences between Two Reverse Sequences as Determined by Solid-State NMR and DFT Calculations.
J Phys Chem B. 2015 Sep 10;119(36):11998-2006
Authors: Karki I, Wang H, Geise NR, Wilson BW, Lewis JP, Gullion T
Abstract
...
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06-14-2016 08:23 PM
[NMR paper] Conformational plasticity of the NNRTI-binding pocket in HIV-1 reverse transcriptase - A fluorine NMR study.
Conformational plasticity of the NNRTI-binding pocket in HIV-1 reverse transcriptase - A fluorine NMR study.
Related Articles Conformational plasticity of the NNRTI-binding pocket in HIV-1 reverse transcriptase - A fluorine NMR study.
Biochemistry. 2016 May 10;
Authors: Sharaf NG, Ishima R, Gronenborn AM
Abstract
HIV-1 reverse transcriptase (RT) is a major drug target in the treatment of HIV-1 infection. RT inhibitors currently in use include non-nucleoside, allosteric RT inhibitors (NNRTIs), which bind to a hydrophobic pocket,...
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[NMR paper] Application of Site-Specific Spin Labeling for NMR Detecting Inhibitor-Induced Conformational Change of HIV-1 Reverse Transcriptase.
Application of Site-Specific Spin Labeling for NMR Detecting Inhibitor-Induced Conformational Change of HIV-1 Reverse Transcriptase.
Related Articles Application of Site-Specific Spin Labeling for NMR Detecting Inhibitor-Induced Conformational Change of HIV-1 Reverse Transcriptase.
ChemMedChem. 2016 Jan 25;
Authors: Seetaha S, Yagi-Utsumi M, Yamaguchi T, Ishii K, Hannongbua S, Choowongkomon K, Kato K
Abstract
Paramagnetism-assisted nuclear magnetic resonance (NMR) techniques can provide long-range structural information...
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01-26-2016 03:40 PM
[NMR paper] NMR assignments of the N-terminal domain of Ogataea polymorpha telomerase reverse transcriptase.
NMR assignments of the N-terminal domain of Ogataea polymorpha telomerase reverse transcriptase.
Related Articles NMR assignments of the N-terminal domain of Ogataea polymorpha telomerase reverse transcriptase.
Biomol NMR Assign. 2015 Dec 31;
Authors: Polshakov VI, Petrova OA, Parfenova YY, Efimov SV, Klochkov VV, Zvereva MI, Dontsova OA
Abstract
Telomerase is a ribonucleoprotein enzyme that adds telomeric DNA fragments to the ends of chromosomes. This enzyme is the focus of substantial attention, both because its structure and...
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[NMR paper] A NMR reverse diffusion filter for the simplification of spectra of complex mixtures and the study of drug receptor interactions.
A NMR reverse diffusion filter for the simplification of spectra of complex mixtures and the study of drug receptor interactions.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary_FullTextOnline_120x27.gif Related Articles A NMR reverse diffusion filter for the simplification of spectra of complex mixtures and the study of drug receptor interactions.
Magn Reson Chem. 2011 Aug;49(8):464-8
Authors: Vega-Vázquez M, Cobas JC, Oliveira de Sousa FF, Martin-Pastor M
...
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Reverse micelles as a platform for dynamic nuclear polarization in solution NMR of proteins
From The DNP-NMR Blog:
Reverse micelles as a platform for dynamic nuclear polarization in solution NMR of proteins
Valentine, K.G., et al., Reverse micelles as a platform for dynamic nuclear polarization in solution NMR of proteins. J Am Chem Soc, 2014. 136(7): p. 2800-7.
http://pubs.acs.org/doi/abs/10.1021/ja4107176
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03-27-2014 03:46 AM
[NMR paper] Reverse micelles as a platform for dynamic nuclear polarization in solution NMR of proteins.
Reverse micelles as a platform for dynamic nuclear polarization in solution NMR of proteins.
Related Articles Reverse micelles as a platform for dynamic nuclear polarization in solution NMR of proteins.
J Am Chem Soc. 2014 Jan 24;
Authors: Valentine KG, Mathies G, Bédard S, Nucci NV, Dodevski I, Stetz MA, Can TV, Griffin RG, Wand AJ
Abstract
Despite tremendous advances in recent years, solution NMR remains fundamentally restricted due to its inherent insensitivity. Dynamic nuclear polarization (DNP) potentially offers significant...
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Modification of Encapsulation Pressure of Reverse Micelles in Liquid Ethane
Modification of Encapsulation Pressure of Reverse Micelles in Liquid Ethane
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 20 June 2011</br>
Ronald W., Peterson , Nathaniel V., Nucci , A., Joshua Wand</br>
A central motivation for employing samples of encapsulated proteins dissolved in low viscosity fluids for high resolution NMR spectroscopy is to benefit from the superior performance afforded by the faster macromolecular rotation of the encapsulated protein than it has in free aqueous solution. Encapsulation of...
NMR characterization of HIV-1 reverse transcriptase binding to various non-nucleoside reverse transcriptase inhibitors with different activities.
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