Figure 5. | RNA-directed remodeling of the HIV-1 protein Rev orchestrates assembly of the Rev–Rev response element complex

Open accessCopyright infoDownload PDFDownload figuresRelated content

RNA-directed remodeling of the HIV-1 protein Rev orchestrates assembly of the Rev–Rev response element complex

Figure 5.

Affiliation details

University of California, San Francisco, United States
Figure 5.
Download figureOpen in new tabFigure 5. Potential diversity of Rev oligomeric structures and functional implications.

Three types of Rev–Rev interactions observed by crystallography, Rev dimers in the RNA-free (Daugherty et al., 2010b) or RNA-bound states (the current structure) and a Rev dimer using the higher-order oligomer interface (DiMattia et al., 2010) are shown within the circle with Rev in grey and the Rev-ARMs in blue. (A) The higher-order oligomer interface was used to combine Rev dimers in the RNA-free state or RNA-bound state in various arrangements to generate examples of hexamers with different architectures. (B) Models illustrating how changes to the RRE structure (red) can alter the architecture of Rev oligomer. Such changes can alter the Rev-RRE ‘jellyfish’ architecture and spatial distribution of NESs, potentially changing their local effective concentration and avidity for the Crm1 dimer (in grey, with RanGTP in light brown and NES-binding sites in yellow), thereby tuning nuclear export activity. Coordinates of the Crm1-RanGTP dimer are from Booth et al., 2014.

DOI: http://dx.doi.org/10.7554/eLife.04120.018