ArticlePloS one2015
Molecular dynamics simulation and experimental verification of the interaction between cyclin T1 and HIV-1 Tat proteins.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Perspectives towards antiviral drug discovery against Ebola virus.Journal of medical virology · 2019Review
- HIV Tat/P-TEFb Interaction: A Potential Target for Novel Anti-HIV Therapies.Molecules (Basel, Switzerland) · 2018Review
- MD simulation of the Tat/Cyclin T1/CDK9 complex revealing the hidden catalytic cavity within the CDK9 molecule upon Tat binding.PloS one · 2017Article
- Determining the role of missense mutations in the POU domain of HNF1A that reduce the DNA-binding affinity: A computational approach.PloS one · 2017Article
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Authors and funding
4 authors.
Funding
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Abstract
The viral encoded Tat protein is essential for the transcriptional activation of HIV proviral DNA. Interaction of Tat with a cellular transcription elongation factor P-TEFb containing CycT1 is critically required for its action. In this study, we performed MD simulation using the 3D data for wild-type and 4CycT1mutants3D data. We found that the dynamic structural change of CycT1 H2' helix is indispensable for its activity for the Tat action. Moreover, we detected flexible structural changes of the Tat-recognition cavity in the WT CycT1 comprising of ten AAs that are in contact with Tat. These structural fluctuations in WT were lost in the CycT1 mutants. We also found the critical importance of the hydrogen bond network involving H1, H1' and H2 helices of CycT1. Since similar AA substitutions of the Tat-CycT1 chimera retained the Tat-supporting activity, these interactions are considered primarily involved in interaction with Tat. These findings described in this paper should provide vital information for the development of effective anti-Tat compound.
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