Document 0261 DOCN M9650261 TI Assignment and modeling of the Rev Response Element RNA bound to a Rev peptide using 13C-heteronuclear NMR. DT 9605 AU Battiste JL; Tan R; Frankel AD; Williamson JR; Department of Chemistry, Massachusetts Institute of Technology,; Cambridge 02139, USA. SO J Biomol NMR. 1995 Dec;6(4):375-89. Unique Identifier : AIDSLINE MED/96141450 AB The Rev Response Element (RRE) RNA-Rev protein interaction is important for regulation of gene expression in the human immunodeficiency virus. A model system for this interaction, which includes stem IIB of the RRE RNA and an arginine-rich peptide from the RNA-binding domain of Rev, was studied using multidimensional heteronuclear NMR. Assignment of the RNA when bound to the peptide was obtained from NMR experiments utilizing uniformly and specifically 13C-labeled RNA. Isotopic filtering experiments on the specifically labeled RNA enable unambiguous assignment of unusual nonsequential NOE patterns present in the internal loop of the RRE. A three-dimensional model of the RNA in the complex was obtained using restrained molecular dynamics calculations. The internal loop contains two purine-purine base pairs, which are stacked to form one continuous helix flanked by two A-form regions. The formation of a G-G base pair in the internal loop requires an unusual structure of the phosphate backbone. This structural feature is consistent with mutational data as being important for the binding of Rev to the RRE. The G-G base pair may play an important role in opening the normally narrow major groove of A-form RNA to permit binding of the Rev basic domain. DE Gene Products, rev/GENETICS/*METABOLISM Genes, env/*GENETICS Human HIV/*GENETICS Models, Molecular Nuclear Magnetic Resonance Nucleic Acid Conformation Protein Binding Protein Conformation RNA, Viral/*GENETICS/METABOLISM Support, Non-U.S. Gov't Support, U.S. Gov't, P.H.S. JOURNAL ARTICLE SOURCE: National Library of Medicine. NOTICE: This material may be protected by Copyright Law (Title 17, U.S.Code).