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      Alpha helix-RNA major groove recognition in an HIV-1 rev peptide-RRE RNA complex.

      Science (New York, N.Y.)
      Amino Acid Sequence, Arginine, chemistry, Asparagine, Base Composition, Base Sequence, DNA-Binding Proteins, Fungal Proteins, Gene Products, rev, metabolism, Genes, env, HIV-1, Hydrogen Bonding, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Nucleic Acid Conformation, Protein Kinases, Protein Structure, Secondary, RNA, Viral, genetics, Saccharomyces cerevisiae Proteins, Threonine, rev Gene Products, Human Immunodeficiency Virus

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          Abstract

          The solution structure of a human immunodeficiency virus type-1 (HIV-1) Rev peptide bound to stem-loop IIB of the Rev response element (RRE) RNA was solved by nuclear magnetic resonance spectroscopy. The Rev peptide has an alpha-helical conformation and binds in the major groove of the RNA near a purine-rich internal loop. Several arginine side chains make base-specific contacts, and an asparagine residue contacts a G.A base pair. The phosphate backbone adjacent to a G.G base pair adopts an unusual structure that allows the peptide to access a widened major groove. The structure formed by the two purine-purine base pairs of the RRE creates a distinctive binding pocket that the peptide can use for specific recognition.

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