ArticleProceedings of the National Academy of Sciences of the United States of America2000
The crystal structure of the Rev binding element of HIV-1 reveals novel base pairing and conformational variability.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- The RNA structural code: orchestrating gene expression and enabling precision therapies.Acta pharmacologica Sinica · 2026Review
- Mutation-driven RRE stem-loop II conformational change induces HIV-1 nuclear export dysfunction.Nucleic acids research · 2025Article
- Structure of HIV-1 RRE stem-loop II identifies two conformational states of the high-affinity Rev binding site.Nature communications · 2024Article
- Structural and computational studies of HIV-1 RNA.RNA biology · 2024Review
- ADAR activation by inducing a syn conformation at guanosine adjacent to an editing site.Nucleic acids research · 2022Article
- Native mass spectrometry reveals the initial binding events of HIV-1 rev to RRE stem II RNA.Nature communications · 2020Article
- Dynamic ensemble of HIV-1 RRE stem IIB reveals non-native conformations that disrupt the Rev-binding site.Nucleic acids research · 2019Article
- m6A minimally impacts the structure, dynamics, and Rev ARM binding properties of HIV-1 RRE stem IIB.PloS one · 2019Article
- Review
- Structural features of a 3' splice site in influenza a.Biochemistry · 2015Article
- The influenza A segment 7 mRNA 3' splice site pseudoknot/hairpin family.RNA biology · 2012Article
- Role of wobble base pair geometry for codon degeneracy: purine-type bases at the anticodon wobble position.Journal of molecular modeling · 2012Article
- Dioxaphosphorinane-constrained nucleic Acid dinucleotides as tools for structural tuning of nucleic acids.Journal of nucleic acids · 2012Article
- The 3' splice site of influenza A segment 7 mRNA can exist in two conformations: a pseudoknot and a hairpin.PloS one · 2012Article
- Extensive purifying selection acting on synonymous sites in HIV-1 Group M sequences.Virology journal · 2008Review
- Noncanonical G(syn)-G(anti) base pairs stabilized by sulphate anions in two X-ray structures of the (GUGGUCUGAUGAGGCC) RNA duplex.RNA (New York, N.Y.) · 2008Article
- The 1.3 A resolution structure of the RNA tridecamer r(GCGUUUGAAACGC): metal ion binding correlates with base unstacking and groove contraction.RNA (New York, N.Y.) · 2007Article
- Base-tetrad swapping results in dimerization of RNA quadruplexes: implications for formation of the i-motif RNA octaplex.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Selenium derivatization and crystallization of DNA and RNA oligonucleotides for X-ray crystallography using multiple anomalous dispersion.Nucleic acids research · 2004Article
- X-ray crystallographic observation of "in-line" and "adjacent" conformations in a bulged self-cleaving RNA/DNA hybrid.RNA (New York, N.Y.) · 2001Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The crystal and molecular structure of an RNA duplex corresponding to the high affinity Rev protein binding element (RBE) has been determined at 2.1-A resolution. Four unique duplexes are present in the crystal, comprising two structural variants. In each duplex, the RNA double helix consists of an annealed 12-mer and 14-mer that form an asymmetric internal loop consisting of G-G and G-A noncanonical base pairs and a flipped-out uridine. The 12-mer strand has an A-form conformation, whereas the 14-mer strand is distorted to accommodate the bulges and noncanonical base pairing. In contrast to the NMR model of the unbound RBE, an asymmetric G-G pair with N2-N7 and N1-O6 hydrogen bonding, is formed in each helix. The G-A base pairing agrees with the NMR structure in one structural variant, but forms a novel water-mediated pair in the other. A backbone flip and reorientation of the G-G base pair is required to assume the RBE conformation present in the NMR model of the complex between the RBE and the Rev peptide.
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