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A long-awaited structure is rev-ealed.

Myles H Hammarskjold¹, David Rekosh

¹Myles H. Thaler Center for AIDS and Human Retrovirus Research and The Department of Microbiology, University of Virginia, Charlottesville, VA 22908, USA.

|September 24, 2011

Summary

New research reveals the flexible RNA binding of the HIV Rev protein and cooperative complex formation with the Rev Response Element (RRE). This structural insight aids in developing therapies against HIV.

Keywords:

HIV-1 RNA export RNA-protein binding RRE Rev X-ray crystallography nuclear-cytoplasmic export protein structure

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Area of Science:

Molecular Biology
Structural Biology
Virology

Background:

The Human Immunodeficiency Virus (HIV) Rev protein is crucial for viral replication.
Rev binds the Rev Response Element (RRE) RNA structure, facilitating nuclear export of viral mRNAs.
This process circumvents host cell restrictions on RNA export.

Purpose of the Study:

To elucidate the structural basis of Rev-RRE complex formation.
To understand the molecular mechanisms of Rev-mediated RNA export.
To identify potential targets for novel anti-HIV drug development.

Main Methods:

High-resolution structural analysis (2.5Å resolution) of the Rev protein and RRE complex.
Investigation of RNA-protein binding flexibility.
Characterization of Rev dimerization and oligomerization interfaces.

Main Results:

Demonstrated flexibility in RNA binding by the Rev arginine-rich motif.
Revealed highly cooperative complex formation involving both Rev protein and RRE.
Defined the structural interfaces for Rev dimerization and oligomerization.

Conclusions:

The findings provide a detailed structural framework for the Rev-RRE interaction.
Understanding this complex is key to inhibiting essential HIV functions.
The structural data enables rational drug design for new HIV therapies.