6H1K
The major G-quadruplex form of HIV-1 LTR
Summary for 6H1K
| Entry DOI | 10.2210/pdb6h1k/pdb |
| NMR Information | BMRB: 34302 |
| Descriptor | DNA (28-MER) (1 entity in total) |
| Functional Keywords | g-quadruplex structure, hiv-1 ltr, stem loop, dna |
| Biological source | Human immunodeficiency virus 1 |
| Total number of polymer chains | 1 |
| Total formula weight | 8865.65 |
| Authors | Phan, A.T.,Heddi, B.,Butovskaya, E.,Bakalar, B.,Richter, S.N. (deposition date: 2018-07-11, release date: 2018-10-17, Last modification date: 2024-06-19) |
| Primary citation | Butovskaya, E.,Heddi, B.,Bakalar, B.,Richter, S.N.,Phan, A.T. Major G-Quadruplex Form of HIV-1 LTR Reveals a (3 + 1) Folding Topology Containing a Stem-Loop. J. Am. Chem. Soc., 140:13654-13662, 2018 Cited by PubMed Abstract: Nucleic acids can form noncanonical four-stranded structures called G-quadruplexes. G-quadruplex-forming sequences are found in several genomes including human and viruses. Previous studies showed that the G-rich sequence located in the U3 promoter region of the HIV-1 long terminal repeat (LTR) folds into a set of dynamically interchangeable G-quadruplex structures. G-quadruplexes formed in the LTR could act as silencer elements to regulate viral transcription. Stabilization of LTR G-quadruplexes by G-quadruplex-specific ligands resulted in decreased viral production, suggesting the possibility of targeting viral G-quadruplex structures for antiviral purposes. Among all the G-quadruplexes formed in the LTR sequence, LTR-III was shown to be the major G-quadruplex conformation in vitro. Here we report the NMR structure of LTR-III in K solution, revealing the formation of a unique quadruplex-duplex hybrid consisting of a three-layer (3 + 1) G-quadruplex scaffold, a 12-nt diagonal loop containing a conserved duplex-stem, a 3-nt lateral loop, a 1-nt propeller loop, and a V-shaped loop. Our structure showed several distinct features including a quadruplex-duplex junction, representing an attractive motif for drug targeting. The structure solved in this study may be used as a promising target to selectively impair the viral cycle. PubMed: 30299955DOI: 10.1021/jacs.8b05332 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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