The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.
Crystal structure of HIV-1 Tat complexed with human P-TEFb
Open accessAbstract
Regulation of the expression of the human immunodeficiency virus (HIV) genome is accomplished in large part by controlling transcription elongation. The viral protein Tat hijacks the host cell's RNA polymerase II elongation control machinery through interaction with the positive transcription elongation factor, P-TEFb, and directs the factor to promote productive elongation of HIV mRNA. Here we describe the crystal structure of the Tat.P-TEFb complex containing HIV-1 Tat, human Cdk9 (also known as CDK9), and human cyclin T1 (also known as CCNT1). Tat adopts a structure complementary to the surface of P-TEFb and makes extensive contacts, mainly with the cyclin T1 subunit of P-TEFb, but also with the T-loop of the Cdk9 subunit. The structure provides a plausible explanation for the tolerance of Tat to sequence variations at certain sites. Importantly, Tat induces significant conformational changes in P-TEFb. This finding lays a foundation for the design of compounds that would specifically inhibit the Tat.P-TEFb complex and block HIV replication.
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“Following the Tat–TAR interaction, the host super elongation complex, which includes the cellular positive transcription elongation factor p-TEFb and polymerase-associated factor 1 (PAF-1), is recruited to further boost transcription, significantly increasing the production of viral RNA transcripts (Fig. 8A) (Peterlin and Price 2006, Tahirov et al. 2010, Gu et al. 2014).”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Tahirov et al. 2010
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Controlling the elongation phase of transcription with P-TEFb
Peterlin, B. M., & Price, D. H. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.014 · Cited by 1,144
Self-citationCrystal structure of the p27Kip1 cyclin-dependent-kinase inibitor bound to the cyclin A–Cdk2 complex
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Transcription elongation factor P-TEFb is required for HIV-1 Tat transactivation in vitroPreprint
Zhu, Y., Peery, T., Peng, J., Ramanathan, Y., Marshall, N. F., Marshall, T. K., Amendt, B. A., Mathews, M. B., & Price, D. H. (1997) · Genes & Development · doi:10.1101/gad.11.20.2622 · Cited by 700
Self-citationControl of RNA Polymerase II Elongation Potential by a Novel Carboxyl-terminal Domain Kinase
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Self-citationGlobal and regional distribution of HIV-1 genetic subtypes and recombinants in 2004
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Flavopiridol Inactivates P-TEFb and Blocks Most RNA Polymerase II Transcription in Vivo
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Deubiquitinase USP8 inhibits HIV-1 replication by suppressing Tat-mediated viral transactivation
Yuan, J., Yang, W., Xu, M., Hu, H., Yang, S., Sun, X., Zhang, W., & Huan, C. (2026) · Journal of Virology · doi:10.1128/jvi.00598-26
Donner, A., 손태빈, Boda, S., Kenney, C. T., Chiandussi, A., Rodríguez, R., Karn, J., & Mbonye, U. R. (2026) · Viruses · doi:10.3390/v18101137
BindingDB (2015) · UC San Diego · doi:10.7270/q28c9xrb
BindingDB (2016) · UC San Diego · doi:10.7270/q2kk9dm6
Metadata
- Authors
- Tahirov, T. H., Babayeva, N. D., Varzavand, K., Cooper, J. J., Sedore, S. C., & Price, D. H.
- Affiliations
- University of Nebraska Medical Center (US)
- University of Iowa (US)
- Corresponding author
- Tahirov, Tahir H.
- Venue
- Nature
- Published
- 2010-06
- Volume
- 465
- Issue
- 7299
- Pages
- 747-751
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC2885016
- OpenAlex
- W2127284613
- Cited by
- 314
- References
- 47
- Citations by year
- 2026: 6 · 2025: 10 · 2024: 13 · 2023: 7 · 2022: 13 · 2021: 10 · 2020: 16 · 2019: 15 · 2018: 25 · 2017: 27 · 2016: 27 · 2015: 24 · 2014: 23 · 2013: 30 · 2012: 28
- FWCI
- 11.16
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- National Institutes of Health
- National Cancer Institute (P30CA036727)
- National Institute of General Medical Sciences (R01GM035500, R01GM082923, GM-35500, GM082923)
- National Institute of Allergy and Infectious Diseases (AI074392, R21AI074392, R33AI074392)
- National Center for Research Resources (RR 15301, P41RR015301)
- Basic Energy Sciences
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
- Keywords
- HIV-1 Tat protein, P-TEFb, CDK9, cyclin T1, transcription elongation, protein-protein interaction, conformational change, HIV replication, antiviral drug targets
- MeSH terms
- Adenosine Triphosphate, Amino Acid Sequence, Animals, Binding Sites, Enzyme Activation, Humans, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Conformation, HIV-1, Crystallography, X-Ray, Cyclin-Dependent Kinase 9, Positive Transcriptional Elongation Factor B, tat Gene Products, Human Immunodeficiency Virus, Cyclin T
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