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spinqualitylabelsall models 1duq, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF THE REV BINDING ELEMENT OF HIV-1

Overview

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 Structure

1DUQ is a Protein complex structure of sequences from [1] with NA as ligand. Full crystallographic information is available from OCA.

Reference

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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