1DUQ
CRYSTAL STRUCTURE OF THE REV BINDING ELEMENT OF HIV-1
Summary for 1DUQ
Entry DOI | 10.2210/pdb1duq/pdb |
Descriptor | THE REV BINDING ELEMENT, SODIUM ION, ... (4 entities in total) |
Functional Keywords | rre, hiv-1, rev binding domain, rna |
Total number of polymer chains | 8 |
Total formula weight | 33766.39 |
Authors | Hung, L.-W.,Holbrook, E.L.,Holbrook, S.R. (deposition date: 2000-01-18, release date: 2000-05-16, Last modification date: 2024-02-07) |
Primary citation | Hung, L.W.,Holbrook, E.L.,Holbrook, S.R. The crystal structure of the Rev binding element of HIV-1 reveals novel base pairing and conformational variability. Proc.Natl.Acad.Sci.USA, 97:5107-5112, 2000 Cited by PubMed Abstract: 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. PubMed: 10792052DOI: 10.1073/pnas.090588197 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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