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.
journal_name
J Struct Bioljournal_title
Journal of structural biologyauthors
Watts NR,Eren E,Zhuang X,Wang YX,Steven AC,Wingfield PTdoi
10.1016/j.jsb.2018.03.011subject
Has Abstractpub_date
2018-08-01 00:00:00pages
102-108issue
2eissn
1047-8477issn
1095-8657pii
S1047-8477(18)30088-1journal_volume
203pub_type
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