RNA architecture dictates the conformations of a bound peptide.

@article{Ye1999RNAAD,
  title={RNA architecture dictates the conformations of a bound peptide.},
  author={X. Ye and A. Gorin and R. Frederick and W. Hu and A. Majumdar and W. Xu and G. Mclendon and A. Ellington and D. Patel},
  journal={Chemistry & biology},
  year={1999},
  volume={6 9},
  pages={
          657-69
        }
}
BACKGROUND The biological function of several viral and bacteriophage proteins, and their arginine-rich subdomains, involves RNA-mediated interactions. It has been shown recently that bound peptides adopt either beta-hairpin or alpha-helical conformations in viral and phage peptide-RNA complexes. We have compared the structures of the arginine-rich peptide domain of HIV-1 Rev bound to two RNA aptamers to determine whether RNA architecture can dictate the conformations of a bound peptide… Expand
75 Citations
Peptide-triggered conformational switch in HIV-1 RRE RNA complexes
  • 56
  • PDF
Structure‐based design of a dimeric RNA–peptide complex
  • 18
  • PDF
Structural characterization of the complex of the Rev response element RNA with a selected peptide.
  • 25
  • PDF
An RNA-binding chameleon.
  • 76
Selection of RRE RNA binding peptides using a kanamycin antitermination assay.
  • 17
  • PDF
Thermodynamics of peptide-RNA recognition: the binding of a Tat peptide to TAR RNA.
  • 34
The arginine-rich RNA-binding motif of HIV-1 Rev is intrinsically disordered and folds upon RRE binding.
  • 36
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 38 REFERENCES
Adaptive recognition in RNA complexes with peptides and protein modules.
  • D. Patel
  • Biology, Medicine
  • Current opinion in structural biology
  • 1999
  • 87
Solution structure of P22 transcriptional antitermination N peptide–box B RNA complex
  • 90
Crystal structure of an RNA aptamer–protein complex at 2.8 Å resolution
  • 118
...
1
2
3
4
...