Model of D-Rev peptide in the complex with RRE IIB. Secondary structures of L-Rev peptide α-helix (A) in complex with RRE IIB (PDB access code 1ETF (8)) and D-Rev β-hairpin models (B,C) are shown as ribbons. D-Rev peptide modeled as a β-hairpin with the turn induced at Arg 42 (model 1, B) and Asn 40 (model 2, C). Residues in D-Rev models (B,C) are numbered accordingly to the positions in the native Rev protein. Residues not involved in RNA interaction are omitted in L-Rev structure (A). Amino acid residues important for RNA binding include Thr 34, Arg 35, Arg 38, Arg 39, Asn 40, or Arg 44, as defined by mutational analysis (Tan and Frankel 1994). The residues that are similarly positioned in L-Rev 34–50 (A) and in D-Rev models (B,C) are shown in color.
