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Implications of the HIV-1 Rev dimer structure at 3.2 Å resolution for multimeric binding to the Rev response element

Academic Article
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Overview

authors

  • DiMattia, M. A.
  • Watts, N. R.
  • Stahl, S. J.
  • Rader, Christoph
  • Wingfield, P. T.
  • Stuart, D. I.
  • Steven, A. C.
  • Grimes, J. M.

publication date

  • March 2010

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • HIV-1 Rev is a small regulatory protein that mediates the nuclear export of viral mRNAs, an essential step in the HIV replication cycle. In this process Rev oligomerizes in association with a highly structured RNA motif, the Rev response element. Crystallographic studies of Rev have been hampered by the protein's tendency to aggregate, but Rev has now been found to form a stable soluble equimolar complex with a specifically engineered monoclonal Fab fragment. We have determined the structure of this complex at 3.2 A resolution. It reveals a molecular dimer of Rev, bound on either side by a Fab, where the ordered portion of each Rev monomer (residues 9-65) contains two coplanar alpha-helices arranged in hairpin fashion. Subunits dimerize through overlapping of the hairpin prongs. Mating of hydrophobic patches on the outer surface of the dimer is likely to promote higher order interactions, suggesting a model for Rev oligomerization onto the viral RNA.

subject areas

  • Antibodies, Monoclonal
  • Crystallography, X-Ray
  • Dimerization
  • Genes, env
  • HIV Antibodies
  • HIV-1
  • Immunoglobulin Fab Fragments
  • Models, Molecular
  • Protein Binding
  • Protein Engineering
  • Protein Structure, Quaternary
  • Recombinant Proteins
  • rev Gene Products, Human Immunodeficiency Virus
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Research

keywords

  • Fab cocrystallization
  • crystal structure
  • nuclear export
  • posttranscriptional regulation
  • ribonucleoprotein structure
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Identity

PubMed Central ID

  • PMC2851902

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.0914946107

PubMed ID

  • 20231488
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Additional Document Info

start page

  • 5810

end page

  • 5814

volume

  • 107

issue

  • 13

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