α Helix-RNA Major Groove Recognition in an HIV-1 Rev Peptide-RRE RNA Complex

Science  13 Sep 1996:
Vol. 273, Issue 5281, pp. 1547-1551
DOI: 10.1126/science.273.5281.1547


The solution structure of a human immunodeficiency virus type-1 (HIV-1) Rev peptide bound to stem-loop IIB of the Rev response element (RRE) RNA was solved by nuclear magnetic resonance spectroscopy. The Rev peptide has an α-helical conformation and binds in the major groove of the RNA near a purine-rich internal loop. Several arginine side chains make base-specific contacts, and an asparagine residue contacts a G·A base pair. The phosphate backbone adjacent to a G·G base pair adopts an unusual structure that allows the peptide to access a widened major groove. The structure formed by the two purine-purine base pairs of the RRE creates a distinctive binding pocket that the peptide can use for specific recognition.

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