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The Human immunodeficiency virus 1 Rev protein (Rev) is a ~13 kDa, 116–amino-acid viral regulatory protein that is essential for HIV-1 replication. Rev binds a structured intronic RNA element, the Rev response element (RRE), and assembles cooperatively as multimers to direct CRM1/Crm1-dependent nuclear export of unspliced and singly spliced viral RNAs needed for production of structural and accessory proteins. Rev contains an N-terminal arginine-rich RNA-binding motif that also serves as a nuclear localization signal and supports oligomerization, and a C-terminal leucine-rich nuclear export signal; structurally, its N-terminal domain forms an antiparallel helix–turn–helix that mediates A–A, B–B, and C–C Rev–Rev interfaces important for higher-order assembly on RRE and filament formation. Beyond canonical RNA export, Rev has been linked to regulation of RNA splicing, stability, translation, and packaging, making it a central, druggable node in the HIV-1 life cycle.
Null (no approved drugs with defined clinical mechanisms against Rev; investigational concepts include disrupting Rev–Rev interfaces, Rev–RRE binding, or Rev–CRM1 interaction).
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