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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.

Original publication




Journal article


Proc Natl Acad Sci U S A

Publication Date





5810 - 5814


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