HIV-1 Nucleocapsid Protein NCp7 and Its RNA Stem Loop 3 Partner: Rotational Dynamics of Spin-Labeled RNA Stem Loop 3†

Biochemistry ◽  
2008 ◽  
Vol 47 (38) ◽  
pp. 10099-10110 ◽  
Author(s):  
Xiangmei Xi ◽  
Yan Sun ◽  
Christine B. Karim ◽  
Vladimir M. Grigoryants ◽  
Charles P. Scholes
Keyword(s):  
Nucleocapsid Protein ◽  
Rotational Dynamics ◽  
Stem Loop ◽  
Labeled Rna ◽  
Hiv 1

Stem-loop SL4 of the HIV-1 Ψ RNA packaging signal exhibits weak affinity for the nucleocapsid protein. structural studies and implications for genome recognition

2001 ◽  
Vol 314 (5) ◽  
pp. 961-970 ◽  
Author(s):  
Gaya K. Amarasinghe ◽  
Jing Zhou ◽  
Matthew Miskimon ◽  
Kalola J. Chancellor ◽  
Jasmine A. McDonald ◽  
...  
Keyword(s):  
Nucleocapsid Protein ◽  
Structural Studies ◽  
Rna Packaging ◽  
Packaging Signal ◽  
Stem Loop ◽  
Genome Recognition ◽  
Rna Packaging Signal ◽  
Hiv 1

NMR structure of the HIV-1 nucleocapsid protein bound to stem-loop SL2 of the Ψ-RNA packaging signal. implications for genome recognition 1 1Edited by P. Wright

2000 ◽  
Vol 301 (2) ◽  
pp. 491-511 ◽  
Author(s):  
Gaya K Amarasinghe ◽  
Roberto N De Guzman ◽  
Ryan B Turner ◽  
Kalola J Chancellor ◽  
Zeng Rong Wu ◽  
...  
Keyword(s):  
Nucleocapsid Protein ◽  
Nmr Structure ◽  
Rna Packaging ◽  
Packaging Signal ◽  
Stem Loop ◽  
Genome Recognition ◽  
Rna Packaging Signal ◽  
Hiv 1

scholarly journals Binding Characteristics of Small Molecules That Mimic Nucleocapsid Protein-Induced Maturation of Stem-Loop 1 of HIV-1 RNA

Biochemistry ◽  
2010 ◽  
Vol 49 (30) ◽  
pp. 6341-6351 ◽  
Author(s):  
Janet Chung ◽  
Nikolai B. Ulyanov ◽  
Christophe Guilbert ◽  
Anwer Mujeeb ◽  
Thomas L. James
Keyword(s):  
Small Molecules ◽  
Nucleocapsid Protein ◽  
Stem Loop ◽  
Binding Characteristics ◽  
Hiv 1

scholarly journals Rotational dynamics of HIV-1 nucleocapsid protein NCp7 as probed by a spin label attached by peptide synthesis

Biopolymers ◽  
2008 ◽  
Vol 89 (12) ◽  
pp. 1125-1135 ◽  
Author(s):  
Zhiwen Zhang ◽  
Xiangmei Xi ◽  
Charles P. Scholes ◽  
Christine B. Karim
Keyword(s):  
Peptide Synthesis ◽  
Spin Label ◽  
Nucleocapsid Protein ◽  
Rotational Dynamics ◽  
Hiv 1

scholarly journals Characterization of the Inhibition Mechanism of HIV-1 Nucleocapsid Protein Chaperone Activities by Methylated Oligoribonucleotides

2011 ◽  
Vol 56 (2) ◽  
pp. 1010-1018 ◽  
Author(s):  
Sergiy V. Avilov ◽  
Christian Boudier ◽  
Marina Gottikh ◽  
Jean-Luc Darlix ◽  
Yves Mély
Keyword(s):  
Dna Synthesis ◽  
Nucleocapsid Protein ◽  
Rational Design ◽  
Early Stage ◽  
Inhibition Mechanism ◽  
Titration Calorimetry ◽  
Viral Dna ◽  
Complementary Sequence ◽  
Stem Loop ◽  
Hiv 1

ABSTRACTSince currently available therapies against HIV/AIDS still show important drawbacks, the development of novel anti-HIV treatments is a key issue. We recently characterized methylated oligoribonucleotides (mONs) that extensively inhibit HIV-1 replication in primary T cells at nanomolar concentrations. The mONs were shown to target both HIV-1 reverse transcriptase (RT) and the nucleocapsid protein (NC), which is an essential partner of RT during viral DNA synthesis. To further understand the mechanism of such mONs, we studied by isothermal titration calorimetry and fluorescence-based techniques their NC binding properties and ability to inhibit the nucleic acid chaperone properties of NC. Notably, we investigated the ability of mONs to inhibit the NC-induced destabilization of the HIV-1 cTAR (complementary DNA sequence to TAR [transactivation response element]) stem-loop and the NC-promoted cTAR annealing to its complementary sequence, required at the early stage of HIV-1 viral DNA synthesis. Moreover, we compared the activity of the mONs to that of a number of modified and nonmodified oligonucleotides. Results show that the mONs inhibit NC by a competitive mechanism whereby the mONs tightly bind the NC peptide, mainly through nonelectrostatic interactions with the hydrophobic platform at the top of the NC zinc fingers. Taken together, these results favor the notion that the mONs impair the process of the RT-directed viral DNA synthesis by sequestering NC molecules, thus preventing the chaperoning of viral DNA synthesis by NC. These findings contribute to the understanding of the molecular basis for NC inhibition by mONs, which could be used for the rational design of antiretroviral compounds targeting HIV-1 NC protein.

Modeling and solution structure probing of the HIV-1 TAR stem-loop

1993 ◽  
Vol 11 (2) ◽  
pp. 92-97 ◽  
Author(s):  
Andrew D. Critchley ◽  
I. Haneef ◽  
Diane J. Cousens ◽  
Peter G. Stockley
Keyword(s):  
Solution Structure ◽  
Stem Loop ◽  
Structure Probing ◽  
Hiv 1
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