HIV-1 Rev NTD dimers with variable crossing angles
Components
Anti-Rev Antibody Fab single-chain variable fragment, light chain,Anti-Rev Antibody Fab single-chain variable fragment, heavy chain
Protein Rev
Keywords
IMMUNE SYSTEM / HIV / helical hairpin / RNA-binding / nuclear export
Function / homology
Function and homology information
protein localization to nucleoplasm / host cell nucleolus / mRNA transport / protein export from nucleus / viral process / host cell cytoplasm / DNA-binding transcription factor activity / RNA binding Similarity search - Function
Journal: Structure / Year: 2016 Title: The Structure of HIV-1 Rev Filaments Suggests a Bilateral Model for Rev-RRE Assembly. 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 / 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.
#256 - Apr 2021 SARS-CoV-2 Spike and Antibodies similarity (1)
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Assembly
Deposited unit
B: Anti-Rev Antibody Fab single-chain variable fragment, light chain,Anti-Rev Antibody Fab single-chain variable fragment, heavy chain C: Protein Rev L: Anti-Rev Antibody Fab single-chain variable fragment, light chain,Anti-Rev Antibody Fab single-chain variable fragment, heavy chain M: Protein Rev
Mass: 26456.133 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Oryctolagus cuniculus (rabbit) / Production host: Escherichia coli (E. coli)
#2: Protein
ProteinRev / ART/TRS / Anti-repression transactivator / Regulator of expression of viral proteins
Mass: 7750.793 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human immunodeficiency virus 1 / Gene: rev / Production host: Escherichia coli (E. coli) / References: UniProt: P69718, UniProt: P04616*PLUS
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION
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Sample preparation
Crystal
Density Matthews: 2.49 Å3/Da / Density % sol: 50.68 %
Crystal grow
Temperature: 293 K / Method: vapor diffusion, sitting drop Details: Crystals of scFv-Rev were initially grown in 20% PEG 3350, a variety of salts (200 mM sodium sulfate, sodium bromide, or ammonium phosphate dibasic), and pH ranging from 6.5-8.5
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