1ETF

REV RESPONSE ELEMENT (RRE) RNA COMPLEXED WITH REV PEPTIDE, NMR, MINIMIZED AVERAGE STRUCTURE

Summary for 1ETF

• Entry DOI: 10.2210/pdb1etf/pdb
• Descriptor: REV RESPONSE ELEMENT RNA, REV PEPTIDE (2 entities in total)
• Functional Keywords: complex (rna-peptide), export regulator, mrna splicing, transcription regulation, viral protein-rna complex, viral protein/rna
• Biological source: Human immunodeficiency virus 1
• Total number of polymer chains: 2
• Total formula weight: 14044.05

Authors

Battiste, J.L.,Mao, H.,Rao, N.S.,Tan, R.,Muhandiram, D.R.,Kay, L.E.,Frankel, A.D.,Willamson, J.R. (deposition date: 1996-08-28, release date: 1997-03-12, Last modification date: 2024-05-22)

Primary citation

Battiste, J.L.,Mao, H.,Rao, N.S.,Tan, R.,Muhandiram, D.R.,Kay, L.E.,Frankel, A.D.,Williamson, J.R.
Alpha helix-RNA major groove recognition in an HIV-1 rev peptide-RRE RNA complex.
Science, 273:1547-1551, 1996

PubMed Abstract: 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 alpha-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.

PubMed: 8703216

Experimental method

SOLUTION NMR