5DHY

HIV-1 Rev NTD dimers with variable crossing angles

5DHY の概要

• エントリーDOI: 10.2210/pdb5dhy/pdb
• 関連するPDBエントリー: 5DHV 5DHX
• 分子名称: Anti-Rev Antibody Fab single-chain variable fragment, heavy chain, Anti-Rev Antibody Fab single-chain variable fragment, light chain, Protein Rev (3 entities in total)
• 機能のキーワード: hiv, helical hairpin, rna-binding, nuclear export, immune system
• 由来する生物種: Oryctolagus cuniculus (Rabbit); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 63975.38

構造登録者

DiMattia, M.A.,Watts, N.R.,Wingfield, P.T.,Grimes, J.M.,Stuart, D.I.,Steven, A.C. (登録日: 2015-08-31, 公開日: 2016-06-22, 最終更新日: 2024-10-09)

主引用文献

DiMattia, M.A.,Watts, N.R.,Cheng, N.,Huang, R.,Heymann, J.B.,Grimes, J.M.,Wingfield, P.T.,Stuart, D.I.,Steven, A.C.
The Structure of HIV-1 Rev Filaments Suggests a Bilateral Model for Rev-RRE Assembly.
Structure, 24:1068-1080, 2016

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 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.

PubMed: 27265851
DOI: 10.1016/j.str.2016.04.015

実験手法

X-RAY DIFFRACTION (3.1 Å)