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• W2186042816 abstract "The Ψ-packaging domain of HIV-1 is used to specify for and control the packaging of, the genomic RNA into a budding immature viron. Interference, through muta- tions and deletions, to the structure of the Ψ-packaging domain, severely diminish the ability of the virus to cor- rectly package genomic RNA. The Gag polypeptide is heavily involved in the binding, coating, trafficking and packaging of genomic RNA, with these processes be- lieved to be initiated by the structural rearrangement of the Ψ-packaging domain, upon binding of Gag. INTRODUCTION, RESULTS AND DISCUSSION, CONCLUSION We investigated the interactions of HIV-1 viral proteins (Gag, NC), with RNA structural motifs within the Ψ- packaging domain of HIV-1 using a systematic incorpora- tion of 2-aminopurine nucleotides. We performed a series of studies aimed at understanding the rearrangement of RNA, by the binding of both Gag and NC (1). The effects of 2- aminopurine substitution on the physical and structural properties of the viral Ψ were characterized. The fluores- cence properties of the 2-aminopurine substitutions showed features consistent with the native GNAR tetraloop (2). Dis- sociation constants (Kd) of the two viral proteins, measured by fluorescence polarization, were similar, and both NC and Gag affected the 2-aminopurine fluorescence of bases close to the loop binding region in a similar fashion. However, the influence of Gag on the fluorescence of the 2-aminopurine nucleotides at the base of the helix implied a much more potent helix destabilizing action on the RNA stem loop (SL) versus that seen with NC. The data are consistent with a model in which the Gag protein has the ability not only to bind to ssRNA, which is a function well established for the NC protein, but also to un- wind the RNA helices to which it binds during the process of genome encapsidation. RNA structure in HIV is highly likely to be dynamic, with different regions adopting differ- ent structures during trafficking through the cell to accom- modate the functional requirements of the RNA at different times (transactivation, nuclear export, translation and pack- aging, etc.) (3). We have also used Gag and a fluorophore-quencher mod- ified RNA within a small molecule screen to identify com- pounds that can interfere with the RNA structural rear- rangement caused by the binding of Gag. Several of the small molecules identified within the small molecule screen are currently showing promising activity within cellular assay and further elucidation of their mode of action is cur- rently on going. Small molecules that can interfere with the packaging of genomic RNA will be valuable tools in further understanding the role of the Ψ-packaging domain as well as validating the domain as a target for a more intense drug discovery program." @default.
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• W2186042816 date "2012-01-01" @default.
• W2186042816 modified "2023-09-27" @default.
• W2186042816 title "UNDERSTANDING AND TARGETING PROTEIN-RNA INTERACTIONS WITHIN THE Ψ- PACKAGING DOMAIN OF HIV-1" @default.
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