Article
An isostructural G-G to A-A substitution within the HIV RRE RNA switches the specificity towards arginine-rich peptides.
Nucleic acids symposium series (2004) - 1 Jan 2009
Aoyama Shoko, Sugaya Maki, Kobayashi Chisato, Masuda Keiko, Maeda Tae, Sakamoto Taiichi, Kawai Gota, Katoh Akira, Harada Kazuo
Abstract excerpt
The HIV Rev protein utilizes a short alpha-helical arginine-rich RNA-binding domain to bind deeply within the major groove of an internal loop region of the Rev-response element (RRE) RNA. A G48-G71 base-pair which covaries to an isostructural A48-A71 base pair has been shown to play an important structure role in Rev-RRE binding. On the other hand, a high affinity RRE-binding peptide aptamer, the K1 peptide, was...
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