ArticleProceedings of the National Academy of Sciences of the United States of America2005
A single intermolecular contact mediates intramolecular stabilization of both RNA and protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 29 citations in OpenAlex.
- Programmable, target-induced fluorogenic CRISPR-tDeg platform for live-cell RNA visualization.Nucleic acids research · 2026Article
- Target-stabilized base editors enable robust high-fidelity RNA editing.Nature communications · 2026Article
- Deep structural insights into RNA-binding disordered protein regions.Wiley interdisciplinary reviews. RNA · 2022Review
- Face-time with TAR: Portraits of an HIV-1 RNA with diverse modes of effector recognition relevant for drug discovery.The Journal of biological chemistry · 2019Review
- Article
- The new (dis)order in RNA regulation.Cell communication and signaling : CCS · 2016Review
- Bovine immunodeficiency virus: a lentiviral infection.Indian journal of virology : an official organ of Indian Virological Society · 2013Article
- Transition step during assembly of HIV Tat:P-TEFb transcription complexes and transfer to TAR RNA.Molecular and cellular biology · 2012Article
- Molecular neuropathogenesis of Alzheimer's disease: an interaction model stressing the central role of oxidative stress.Future neurology · 2012Article
- Comparative functional analysis of Jembrana disease virus Tat protein on lentivirus long terminal repeat promoters: evidence for flexibility at its N-terminus.Virology journal · 2009Article
- Tat acetylation modulates assembly of a viral-host RNA-protein transcription complex.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- An approach to the construction of tailor-made amphiphilic peptides that strongly and selectively bind to hairpin RNA targets.Journal of the American Chemical Society · 2009Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
An arginine-rich peptide from the Jembrana disease virus (JDV) Tat protein is a structural "chameleon" that binds bovine immunodeficiency virus (BIV) or HIV TAR RNAs in two different binding modes, with an affinity for BIV TAR even higher than the cognate BIV peptide. We determined the NMR structure of the JDV Tat-BIV TAR high-affinity complex and found that the C-terminal tyrosine in JDV Tat forms a network of inter- and intramolecular hydrogen bonding and stacking interactions that simultaneously stabilize the beta-hairpin conformation of the peptide and a base triple in the RNA. A neighboring histidine also appears to help stabilize the peptide conformation. Induced fit binding is recurrent in protein-protein and protein-nucleic acid interactions, and the JDV Tat complex demonstrates how high affinity can be achieved not only by optimization of the binding interface but also by inducing new intramolecular contacts that stabilize each binding partner. Comparison to the cognate BIV Tat peptide-TAR complex shows how such a costabilization mechanism can evolve with only small changes to the peptide sequence. In addition, the bound structure of BIV TAR in the chameleon peptide complex is strikingly similar to the bound conformation of HIV TAR, suggesting new strategies for the development of HIV TAR binding molecules.
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Registered trials
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.