7DO1
Solution structure of a heteromolecular telomeric (3+1) G-quadruplex containing right loop progression
Summary for 7DO1
Entry DOI | 10.2210/pdb7do1/pdb |
Descriptor | DNA (5'-D(*GP*GP*GP*TP*TP*AP*GP*GP*GP*TP*TP*AP*GP*GP*G)-3'), DNA (5'-D(*TP*TP*AP*GP*GP*G)-3') (2 entities in total) |
Functional Keywords | hybrid g-quadruplex, human telomere, (3+1), dna |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 2 |
Total formula weight | 6625.33 |
Authors | Fu, W.Q.,Jing, H.T.,Zhang, N. (deposition date: 2020-12-11, release date: 2021-09-29, Last modification date: 2024-05-15) |
Primary citation | Fu, W.,Jing, H.,Xu, X.,Xu, S.,Wang, T.,Hu, W.,Li, H.,Zhang, N. Two coexisting pseudo-mirror heteromolecular telomeric G-quadruplexes in opposite loop progressions differentially recognized by a low equivalent of Thioflavin T. Nucleic Acids Res., 49:10717-10734, 2021 Cited by PubMed Abstract: The final 3'-terminal residue of the telomeric DNA G-overhang is inherently less precise. Here, we describe how alteration of the last 3'-terminal base affects the mutual recognition between two different G-rich oligomers of human telomeric DNA in the formation of heteromolecular G-quadruplexes (hetero-GQs). Associations between three- and single-repeat fragments of human telomeric DNA, target d(GGGTTAGGGTTAGGG) and probe d(TAGGGT), in Na+ solution yield two coexisting forms of (3 + 1) hybrid hetero-GQs: the kinetically favourable LLP-form (left loop progression) and the thermodynamically controlled RLP-form (right loop progression). However, only the adoption of a single LLP-form has been previously reported between the same probe d(TAGGGT) and a target variant d(GGGTTAGGGTTAGGGT) having one extra 3'-end thymine. Moreover, the flanking base alterations of short G-rich probe variants also significantly affect the loop progressions of hetero-GQs. Although seemingly two pseudo-mirror counter partners, the RLP-form exhibits a preference over the LLP-form to be recognized by a low equivalent of fluorescence dye thioflavin T (ThT). To a greater extent, ThT preferentially binds to RLP hetero-GQ than with the corresponding telomeric DNA duplex context or several other representative unimolecular GQs. PubMed: 34500466DOI: 10.1093/nar/gkab755 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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