2N4Y
Structure and possible function of a G-quadruplex in the long terminal repeat of the proviral HIV-1 genome
Summary for 2N4Y
Entry DOI | 10.2210/pdb2n4y/pdb |
NMR Information | BMRB: 25686 |
Descriptor | DNA_(5'-D(*CP*TP*GP*GP*GP*CP*GP*GP*GP*AP*CP*TP*GP*GP*GP*GP*AP*GP*TP*GP*GP*T)-3') (1 entity in total) |
Functional Keywords | g-quadruplex, hiv-1, long terminal repeat, dna |
Biological source | synthetic construct |
Total number of polymer chains | 1 |
Total formula weight | 6945.45 |
Authors | DeNicola, B.,Lech, C.J.,Heddi, B.,Regmi, S.,Frasson, I.,Perrone, R.,Richter, S.N.,Phan, A.T. (deposition date: 2015-07-02, release date: 2016-06-29, Last modification date: 2024-05-15) |
Primary citation | De Nicola, B.,Lech, C.J.,Heddi, B.,Regmi, S.,Frasson, I.,Perrone, R.,Richter, S.N.,Phan, A.T. Structure and possible function of a G-quadruplex in the long terminal repeat of the proviral HIV-1 genome. Nucleic Acids Res., 44:6442-6451, 2016 Cited by PubMed Abstract: The long terminal repeat (LTR) of the proviral human immunodeficiency virus (HIV)-1 genome is integral to virus transcription and host cell infection. The guanine-rich U3 region within the LTR promoter, previously shown to form G-quadruplex structures, represents an attractive target to inhibit HIV transcription and replication. In this work, we report the structure of a biologically relevant G-quadruplex within the LTR promoter region of HIV-1. The guanine-rich sequence designated LTR-IV forms a well-defined structure in physiological cationic solution. The nuclear magnetic resonance (NMR) structure of this sequence reveals a parallel-stranded G-quadruplex containing a single-nucleotide thymine bulge, which participates in a conserved stacking interaction with a neighboring single-nucleotide adenine loop. Transcription analysis in a HIV-1 replication competent cell indicates that the LTR-IV region may act as a modulator of G-quadruplex formation in the LTR promoter. Consequently, the LTR-IV G-quadruplex structure presented within this work could represent a valuable target for the design of HIV therapeutics. PubMed: 27298260DOI: 10.1093/nar/gkw432 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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