Summary information and primary citation

PDB-id
4pmi; SNAP-derived features in text and JSON formats; DNAproDB
Class
RNA binding protein-RNA
Method
X-ray (3.2 Å)
Summary
Crystal structure of rev and rev-response-element RNA complex
Reference
Jayaraman B, Crosby DC, Homer C, Ribeiro I, Mavor D, Frankel AD (2014): "RNA-directed remodeling of the HIV-1 protein Rev orchestrates assembly of the Rev-Rev response element complex." Elife, 4, e04120. doi: 10.7554/eLife.04120.
Abstract
The HIV-1 protein Rev controls a critical step in viral replication by mediating the nuclear export of unspliced and singly-spliced viral mRNAs. Multiple Rev subunits assemble on the Rev Response Element (RRE), a structured region present in these RNAs, and direct their export through the Crm1 pathway. Rev-RRE assembly occurs via several Rev oligomerization and RNA-binding steps, but how these steps are coordinated to form an export-competent complex is unclear. Here, we report the first crystal structure of a Rev dimer-RRE complex, revealing a dramatic rearrangement of the Rev-dimer upon RRE binding through re-packing of its hydrophobic protein-protein interface. Rev-RNA recognition relies on sequence-specific contacts at the well-characterized IIB site and local RNA architecture at the second site. The structure supports a model in which the RRE utilizes the inherent plasticity of Rev subunit interfaces to guide the formation of a functional complex.

Cartoon-block schematics in six views (download the tarball)

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