1ULL

RNA APTAMER COMPLEXED WITH HIV-1 REV PEPTIDE, NMR, 7 STRUCTURES

Summary for 1ULL

• Entry DOI: 10.2210/pdb1ull/pdb
• Descriptor: RNA (5'-R (GP*GP*CP*UP*GP*GP*AP*CP*UP*CP*GP*UP*AP*CP*UP*UP*CP*GP* GP*UP*AP*CP*UP*GP*GP*AP*GP*AP*AP*AP*CP*AP*GP*CP*C)-3'), REV PEPTIDE (2 entities in total)
• Functional Keywords: rev peptide-rna recognition, alpha-helix in widened rna major groove, purine-purine mismatches, uau base triple, adaptive binding of peptide and rna in complex, complex (rna aptamer-rev peptide), viral protein-rna complex, viral protein/rna
• Biological source: Human immunodeficiency virus 1; More
• Cellular location: Host nucleus, host nucleolus: P05866
• Total number of polymer chains: 2
• Total formula weight: 13723.57

Authors

Ye, X.,Gorin, A.,Ellington, A.D.,Patel, D.J. (deposition date: 1996-11-05, release date: 1997-08-20, Last modification date: 2024-05-22)

Primary citation

Ye, X.,Gorin, A.,Ellington, A.D.,Patel, D.J.
Deep penetration of an alpha-helix into a widened RNA major groove in the HIV-1 rev peptide-RNA aptamer complex.
Nat.Struct.Biol., 3:1026-1033, 1996

PubMed Abstract: A combined NMR-molecular dynamics approach has been applied to determine the solution structure of a HIV-1 17-mer rev peptide bound to its 35-mer high affinity RNA aptamer binding site. Complex formation involves adaptive binding with the alpha-helical arginine-rich basic rev peptide targeting a widened RNA major groove centred about adjacent G.A and reversed A.A mismatches. We have also identified a U AU triple in the aptamer complex with the Hoogsteen-paired uracil base sandwiched between two arginine side chains. The intermolecular contacts identified in the aptamer complex readily account for the consequences of peptide and RNA mutations, as well as the results of previous in vitro selection experiments. The details of molecular recognition associated with targeting by rev of its high affinity RNA binding sites open new opportunities for structure-based drug design strategies.

PubMed: 8946856
DOI: 10.1038/nsb1296-1026

Experimental method

SOLUTION NMR