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

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

SUBMITTER: DiMattia MA 

PROVIDER: S-EPMC2851902 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature