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- W2063552135 abstract "Basic peptides from the carboxy terminus of the HIV-1 Tat protein bind to the apical stem-loop region of TAR RNA with high affinity and moderate specificity. The conformations of the unbound and 24 residue Tat peptide (Tfr24)-bound forms of TAR RNA have been characterized by NMR spectroscopy. The unbound form of TAR exists in major and minor forms having different trinucleotide bulge conformations. A specific TAR RNA conformational change is observed upon complex formation with Tfr24, consisting of coaxial stacking of helical stems and base triple formation. A U23-A27-U38 base triple is proposed based on exchangeable proton NMR data, where U23 forms a base pair with A27 in the major groove. No evidence for base triple formation was found for Tat peptides in which lysine residues are extensively substituted for arginine." @default.
- W2063552135 created "2016-06-24" @default.
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- W2063552135 date "1999-07-10" @default.
- W2063552135 modified "2023-09-26" @default.
- W2063552135 title "Characterization of the Solution Conformations of Unbound and Tat Peptide-Bound Forms of HIV-1 TAR RNA" @default.
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- W2063552135 doi "https://doi.org/10.1021/bi990590h" @default.
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