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Title | The Structure of HIV-1 Rev Filaments Suggests a Bilateral Model for Rev-RRE Assembly. |
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Journal, issue, pages | Structure, Vol. 24, Issue 7, Page 1068-1080, Year 2016 |
Publish date | Jul 6, 2016 |
Authors | Michael A DiMattia / Norman R Watts / Naiqian Cheng / Rick Huang / J Bernard Heymann / Jonathan M Grimes / Paul T Wingfield / David I Stuart / Alasdair C Steven / |
PubMed Abstract | HIV-1 Rev protein mediates the nuclear export of viral RNA genomes. To do so, Rev oligomerizes cooperatively onto an RNA motif, the Rev response element (RRE), forming a complex that engages with the ...HIV-1 Rev protein mediates the nuclear export of viral RNA genomes. To do so, Rev oligomerizes cooperatively onto an RNA motif, the Rev response element (RRE), forming a complex that engages with the host nuclear export machinery. To better understand Rev oligomerization, we determined four crystal structures of Rev N-terminal domain dimers, which show that they can pivot about their dyad axis, giving crossing angles of 90° to 140°. In parallel, we performed cryoelectron microscopy of helical Rev filaments. Filaments vary from 11 to 15 nm in width, reflecting variations in dimer crossing angle. These structures contain additional density, indicating that C-terminal domains become partially ordered in the context of filaments. This conformational variability may be exploited in the assembly of RRE/Rev complexes. Our data also revealed a third interface between Revs, which offers an explanation for how the arrangement of Rev subunits adapts to the "A"-shaped architecture of the RRE in export-active complexes. |
External links | Structure / PubMed:27265851 / PubMed Central |
Methods | EM (helical sym.) / X-ray diffraction |
Resolution | 2.3 - 8.3 Å |
Structure data | EMDB-6439: PDB-5dhv: PDB-5dhx: PDB-5dhy: PDB-5dhz: |
Chemicals | ChemComp-CL: ChemComp-HOH: |
Source |
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Keywords | IMMUNE SYSTEM / HIV / helical hairpin / RNA-binding / nuclear export |