ArticleNucleic acids research2006
TAR-RNA recognition by a novel cyclic aminoglycoside analogue.
Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 29 citations in OpenAlex.
- Exploring the Druggability of Conserved RNA Regulatory Elements in the SARS-CoV-2 Genome.Angewandte Chemie (International ed. in English) · 2021Article
- An eco-compatible strategy for the diversity-oriented synthesis of macrocycles exploiting carbohydrate-derived building blocks.Beilstein journal of organic chemistry · 2017Article
- Multivalent Amino Sugars to Recognize Different TAR RNA Conformations.MedChemComm · 2014Article
- Recognition of viral RNA stem-loops by the tandem double-stranded RNA binding domains of PKR.RNA (New York, N.Y.) · 2013Article
- Click dimers to target HIV TAR RNA conformation.Biochemistry · 2012Article
- A small-molecule probe induces a conformation in HIV TAR RNA capable of binding drug-like fragments.Journal of molecular biology · 2011Article
- Essential structural requirements for specific recognition of HIV TAR RNA by peptide mimetics of Tat protein.Nucleic acids research · 2011Article
- Binding of aminoglycoside antibiotics to helix 69 of 23S rRNA.Nucleic acids research · 2010Article
- Simultaneous recognition of HIV-1 TAR RNA bulge and loop sequences by cyclic peptide mimics of Tat protein.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Structure of the cytosine-cytosine mismatch in the thymidylate synthase mRNA binding site and analysis of its interaction with the aminoglycoside paromomycin.RNA (New York, N.Y.) · 2009Article
- Aminoglycosides: molecular insights on the recognition of RNA and aminoglycoside mimics.Perspectives in medicinal chemistry · 2009Article
- Binding sites of the viral RNA element TAR and of TAR mutants for various peptide ligands, probed with LILBID: a new laser mass spectrometry.Journal of the American Society for Mass Spectrometry · 2008Article
- Characterizing complex dynamics in the transactivation response element apical loop and motional correlations with the bulge by NMR, molecular dynamics, and mutagenesis.Biophysical journal · 2008Article
- Guanidinoneomycin B recognition of an HIV-1 RNA helix.Chembiochem : a European journal of chemical biology · 2008Article
- Scanning conformational space with a library of stereo- and regiochemically diverse aminoglycoside derivatives: the discovery of new ligands for RNA hairpin sequences.Organic & biomolecular chemistry · 2007Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The formation of the Tat-protein/TAR-RNA complex is a crucial step in the regulation of human immunodeficiency virus (HIV)-gene expression. To obtain full-length viral transcripts the Tat/TAR complex has to recruit the positive transcription elongation factor complex (P-EFTb), which interacts with TAR through its cyclin T1 (CycT1) component. Mutational studies identified the TAR hexanucleotide loop as a crucial region for contacting CycT1. Interfering with the interaction between the Tat/CycT1 complex and the TAR-RNA is an attractive strategy for the design of anti-HIV drugs. Positively charged molecules, like aminoglycosides or peptidomimetics, bind the TAR-RNA, disrupting the Tat/TAR complex. Here, we investigate the complex between the HIV-2 TAR-RNA and a neooligoaminodeoxysaccharide by NMR spectroscopy. In contrast to other aminoglycosides, this novel aminoglycoside analogue contacts simultaneously the bulge residues required for Tat binding and the A35 residue of the hexanucleotide loop. Upon complex formation, the loop region undergoes profound conformational changes. The novel binding mode, together with the easy accessibility of derivatives for the neooligoaminodeoxysaccharide, could open the way to the design of a new class of TAR-RNA binders, which simultaneously inhibit the formation of both the Tat/TAR binary complex and the Tat/TAR/CycT1 ternary complex by obstructing both the bulge and loop regions of the RNA.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.