The Structure of HIV-1 Rev Filaments Suggests a Bilateral Model for Rev-RRE Assembly.

摘要: Summary HIV-1 Rev protein mediates the nuclear export of viral RNA genomes. To do so, oligomerizes cooperatively onto an motif, response element (RRE), forming a complex that engages with host machinery. better understand oligomerization, we determined four crystal structures N-terminal domain dimers, which show they can pivot about their dyad axis, giving crossing angles 90° to 140°. In parallel, performed cryoelectron microscopy helical filaments. Filaments vary from 11 15 nm in width, reflecting variations dimer angle. These contain additional density, indicating C-terminal domains become partially ordered context This conformational variability may be exploited assembly RRE/Rev complexes. Our data also revealed third interface between Revs, offers explanation for how arrangement subunits adapts "A"-shaped architecture RRE export-active