The solution NMR structure of the isolated thumb subdomain of HIV-1 reverse transcriptase (RT)Â*has been determined. A detailed comparison of the current structure with dozens of the highest resolution crystal structures of this domain in the context of the full-length enzyme reveals that the overall structures are very similar, with only two regions exhibiting local conformational differences. The C-terminal capping pattern of the αH helix is subtly different, and the loop connecting the αI and αJ helices in the p51 chain of the full-length p51/p66 heterodimeric RT differs from our NMR structure due to unique packing interactions in mature RT. Overall, our data show that the thumb subdomain folds independently and essentially the same in isolation as in its natural structural context.
[NMR paper] NMR characterization of HIV-1 reverse transcriptase binding to various non-nucleoside reverse transcriptase inhibitors with different activities.
NMR characterization of HIV-1 reverse transcriptase binding to various non-nucleoside reverse transcriptase inhibitors with different activities.
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.gif Related Articles NMR characterization of HIV-1 reverse transcriptase binding to various non-nucleoside reverse transcriptase inhibitors with different activities.
Sci Rep. 2015;5:15806
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[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] NMR Characterization and Membrane Interactions of the Loop Region of Kindlin-3 F1 Subdomain.
NMR Characterization and Membrane Interactions of the Loop Region of Kindlin-3 F1 Subdomain.
Related Articles NMR Characterization and Membrane Interactions of the Loop Region of Kindlin-3 F1 Subdomain.
PLoS One. 2016;11(4):e0153501
Authors: Chua GL, Tan SM, Bhattacharjya S
Abstract
Kindlins-1,2 and 3 are FERM domain-containing cytosolic proteins involved in the activation and regulation of integrin-mediated cell adhesion. Apart from binding to integrin ? cytosolic tails, kindlins and the well characterized integrin-activator...
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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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[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] Refining the overall structure and subdomain orientation of ribosomal protein S4 delt
Refining the overall structure and subdomain orientation of ribosomal protein S4 delta41 with dipolar couplings measured by NMR in uniaxial liquid crystalline phases.
Related Articles Refining the overall structure and subdomain orientation of ribosomal protein S4 delta41 with dipolar couplings measured by NMR in uniaxial liquid crystalline phases.
J Mol Biol. 1999 Sep 17;292(2):375-87
Authors: Markus MA, Gerstner RB, Draper DE, Torchia DA
Prokaryotic protein S4 initiates assembly of the small ribosomal subunit by binding to 16 S rRNA....
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[NMR paper] Dissection of the basic subdomain of the c-Jun oncoprotein: a structural analysis of
Dissection of the basic subdomain of the c-Jun oncoprotein: a structural analysis of two peptide fragments by CD, Fourier-transform infrared and NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Dissection of the basic subdomain of the c-Jun oncoprotein: a structural analysis of two peptide fragments by CD, Fourier-transform infrared and NMR.
Eur J Biochem. 1996 Feb 1;235(3):699-712
Authors: Krebs D, Dahmani B, Monnot M, Mauffret O,...
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[NMR paper] The basic subdomain of the c-Jun oncoprotein. A joint CD, Fourier-transform infrared
The basic subdomain of the c-Jun oncoprotein. A joint CD, Fourier-transform infrared and NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles The basic subdomain of the c-Jun oncoprotein. A joint CD, Fourier-transform infrared and NMR study.
Eur J Biochem. 1995 Jul 15;231(2):370-80
Authors: Krebs D, Dahmani B, el Antri S, Monnot M, Convert O, Mauffret O, Troalen F, Fermandjian S
The structural properties of the basic...