Cited by 314HIV Research and TreatmentGenomics and Chromatin DynamicsHIV/AIDS drug development and treatment

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Crystal structure of HIV-1 Tat complexed with human P-TEFb

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Tahirov, Tahir H., Babayeva, Nigar D., Varzavand, Katayoun, Cooper, Jeffrey J., Sedore, Stanley C., Price, David H.·2010·Nature

DOI 10.1038/nature09131PMC PMC2885016

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Abstract

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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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.
ORCID: Tahirov, Tahir H.
Babayeva, Nigar D.
Price, David H.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2010-06
Volume: 465
Issue: 7299
Pages: 747-751
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature09131
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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Crystal structure of HIV-1 Tat complexed with human P-TEFb

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