Summary for 1EXY
| Entry DOI | 10.2210/pdb1exy/pdb |
| Descriptor | RNA APTAMER, 33-MER, HTLV-1 REX PEPTIDE (2 entities in total) |
| Functional Keywords | arginine-guanine sandwich, extended bound basic rex peptide, flap base, junctional base triplets, rna binding pocket architecture, rna binding protein-rna complex, rna binding protein/rna |
| Total number of polymer chains | 2 |
| Total formula weight | 12769.99 |
| Authors | Jiang, F.,Gorin, A.,Hu, W.,Majumdar, A.,Baskerville, S.,Xu, W.,Ellington, A.,Patel, D.J. (deposition date: 2000-05-05, release date: 2000-05-15, Last modification date: 2024-05-22) |
| Primary citation | Jiang, F.,Gorin, A.,Hu, W.,Majumdar, A.,Baskerville, S.,Xu, W.,Ellington, A.,Patel, D.J. Anchoring an extended HTLV-1 Rex peptide within an RNA major groove containing junctional base triples. Structure Fold.Des., 7:1461-1472, 1999 Cited by 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. PubMed: 10647177DOI: 10.1016/S0969-2126(00)88337-9 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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