6BSY

HIV-1 Rev assembly domain (residues 1-69)

Summary for 6BSY

• Entry DOI: 10.2210/pdb6bsy/pdb
• Related: 2X7L
• Descriptor: Protein Rev, PHOSPHATE ION (3 entities in total)
• Functional Keywords: hiv, rev, viral protein
• Biological source: Human immunodeficiency virus 1
• Total number of polymer chains: 2
• Total formula weight: 16679.71

Authors

Watts, N.R.,Eren, E.,Zhuang, X.,Wang, Y.X.,Steven, A.C.,Wingfield, P.T. (deposition date: 2017-12-04, release date: 2018-04-11, Last modification date: 2023-10-04)

Primary citation

Watts, N.R.,Eren, E.,Zhuang, X.,Wang, Y.X.,Steven, A.C.,Wingfield, P.T.
A new HIV-1 Rev structure optimizes interaction with target RNA (RRE) for nuclear export.
J. Struct. Biol., 203:102-108, 2018

PubMed Abstract: HIV-1 Rev mediates the nuclear export of unspliced and partially-spliced viral transcripts for the production of progeny genomes and structural proteins. In this process, four (or more) copies of Rev assemble onto a highly-structured 351-nt region in such viral transcripts, the Rev response element (RRE). How this occurs is not known. The Rev assembly domain has a helical-hairpin structure which associates through three (A-A, B-B and C-C) interfaces. The RRE has the topology of an upper-case letter A, with the two known Rev binding sites mapping onto the legs of the A. We have determined a crystal structure for the Rev assembly domain at 2.25 Å resolution, without resort to either mutations or chaperones. It shows that B-B dimers adopt an arrangement reversed relative to that previously reported, and join through a C-C interface to form tetramers. The new subunit arrangement shows how four Rev molecules can assemble on the two sites on the RRE to form the specificity checkpoint, and how further copies add through A-A interactions. Residues at the C-C interface, specifically the Pro31-Trp45 axis, are a potential target for intervention.

PubMed: 29605570
DOI: 10.1016/j.jsb.2018.03.011

Experimental method

X-RAY DIFFRACTION (2.25 Å)