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

Academic Article
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Overview

authors

  • Battiste, J. L.
  • Mao, H. Y.
  • Rao, N. S.
  • Tan, R. Y.
  • Muhandiram, D. R.
  • Kay, L. E.
  • Frankel, A. D.
  • Williamson, James

publication date

  • September 1996

journal

  • Science  Journal

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.

subject areas

  • Amino Acid Sequence
  • Arginine
  • Asparagine
  • Base Composition
  • Base Sequence
  • DNA-Binding Proteins
  • Fungal Proteins
  • Gene Products, rev
  • Genes, env
  • HIV-1
  • Hydrogen Bonding
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Protein Kinases
  • Protein Structure, Secondary
  • RNA, Viral
  • Saccharomyces cerevisiae Proteins
  • Threonine
  • rev Gene Products, Human Immunodeficiency Virus
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Identity

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.273.5281.1547

PubMed ID

  • 8703216
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Additional Document Info

start page

  • 1547

end page

  • 1551

volume

  • 273

issue

  • 5281

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