+検索条件
-Structure paper
タイトル | The Structure of HIV-1 Rev Filaments Suggests a Bilateral Model for Rev-RRE Assembly. |
---|---|
ジャーナル・号・ページ | Structure, Vol. 24, Issue 7, Page 1068-1080, Year 2016 |
掲載日 | 2016年7月6日 |
![]() | 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 要旨 | 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. |
![]() | ![]() ![]() ![]() |
手法 | EM (らせん対称) / X線回折 |
解像度 | 2.3 - 8.3 Å |
構造データ | ![]() EMDB-6439: ![]() PDB-5dhv: ![]() PDB-5dhx: ![]() PDB-5dhy: ![]() PDB-5dhz: |
化合物 | ![]() ChemComp-CL: ![]() ChemComp-HOH: |
由来 |
|
![]() | ![]() ![]() ![]() |