Download MendeleyAnchoring an extended HTLV-1 Rex peptide within an RNA major groove containing junctional base triples.
Jiang, F., Gorin, A., Hu, W., Majumdar, A., Baskerville, S., Xu, W., Ellington, A., Patel, D.J.(1999) Structure 7: 1461-1472
- PubMed: 10647177
- DOI: https://doi.org/10.1016/s0969-2126(00)88337-9
- Primary Citation of Related Structures:
1EXY - PubMed Abstract:
The Rex protein of the human T cell leukemia virus type 1 (HTLV-1) belongs to a family of proteins that use arginine-rich motifs (ARMs) to recognize their RNA targets. Previously, an in vitro selected RNA aptamer sequence was identified that mediates mRNA transport in vivo when placed in the primary binding site on stem-loop IID of the Rex response element. We present the solution structure of the HTLV-1 arginine-rich Rex peptide bound to its RNA aptamer target determined by multidimensional heteronuclear NMR spectroscopy.
Organizational Affiliation:
Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.
