1duq
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CRYSTAL STRUCTURE OF THE REV BINDING ELEMENT OF HIV-1
OverviewOverview
The crystal and molecular structure of an RNA duplex corresponding to the, high affinity Rev protein binding element (RBE) has been determined at, 2.1-A resolution. Four unique duplexes are present in the crystal, comprising two structural variants. In each duplex, the RNA double helix, consists of an annealed 12-mer and 14-mer that form an asymmetric internal, loop consisting of G-G and G-A noncanonical base pairs and a flipped-out, uridine. The 12-mer strand has an A-form conformation, whereas the 14-mer, strand is distorted to accommodate the bulges and noncanonical base, pairing. In contrast to the NMR model of the unbound RBE, an asymmetric, G-G pair with N2-N7 and N1-O6 hydrogen bonding, is formed in each helix., The G-A base pairing agrees with the NMR structure in one structural, variant, but forms a novel water-mediated pair in the other. A backbone, flip and reorientation of the G-G base pair is required to assume the RBE, conformation present in the NMR model of the complex between the RBE and, the Rev peptide.
About this StructureAbout this Structure
1DUQ is a Protein complex structure of sequences from [1] with NA as ligand. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of the Rev binding element of HIV-1 reveals novel base pairing and conformational variability., Hung LW, Holbrook EL, Holbrook SR, Proc Natl Acad Sci U S A. 2000 May 9;97(10):5107-12. PMID:10792052
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