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April 22, 2026PLoS ONEOpen Access

Effect of HIV-1 subtype-specific Tat protein polymorphisms on Tat-TAR interaction

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Authors

AZAlnara ZhamalbekovaMIMahmoud A. A. IbrahimPSPeter A. Sidhom

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Overview

This investigation identifies subtype-specific polymorphisms influencing Tat-TAR interactions, suggesting implications for disease pathogenesis.

Key Points

  • The study aims to explore how polymorphisms in HIV-1 Tat protein from different subtypes affect its interaction with TAR RNA.
  • Retrieval of HIV Tat protein sequences from multiple subtypes.
  • Alignment and generation of consensus sequences to identify polymorphisms.
  • 3D modeling and molecular simulations to assess binding affinities with TAR.
  • Subtypes A6, C, and CRF02_AG show high binding affinities for TAR (–126.8 to –123.2 kcal/mol).
  • Subtypes A3 and A1 demonstrate weak binding affinities (–63.3 and –57.5 kcal/mol).
  • Specific polymorphisms in Tat protein contribute to the differences in binding affinities among subtypes.

Cite This Study

Zhamalbekova et al. (2026) studied this question.

synapsesocial.com/papers/69e865fd6e0dea528ddea6ffhttps://doi.org/10.1371/journal.pone.0346629
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Analysis of the effect of HIV-1 subtype-specific Tat polymorphisms on Tat-TAR interaction2024 · 1 citations
  2. 2Impact of subtype C-specific amino acid variants on HIV-1 Tat-TAR interaction: insights from molecular modelling and dynamics2024 · 5 citations
  3. 3A multi-residue electrostatic clamp in HIV-1 CRF01_AE Tat underlies high-affinity engagement with NMDA and hDAT receptors2026
  4. 4Functional comparison of the basic domains of the Tat proteins of human immunodeficiency virus types 1 and 2 in trans activation1992 · 23 citations
  5. 5The number of positively charged amino acids in the basic domain of Tat is critical for trans-activation and complex formation with TAR RNA.1991 · 77 citations