3R1C
Crystal structure of GCGGCGGC duplex
Summary for 3R1C
| Entry DOI | 10.2210/pdb3r1c/pdb |
| Related | 3R1D 3R1E |
| Descriptor | RNA (5'-R(*GP*CP*GP*GP*CP*GP*GP*C)-3'), SULFATE ION (3 entities in total) |
| Functional Keywords | cgg repeats, fragile x mental retardation, rna |
| Total number of polymer chains | 36 |
| Total formula weight | 94150.65 |
| Authors | Kiliszek, A.,Kierzek, R.,Krzyzosiak, W.J.,Rypniewski, W. (deposition date: 2011-03-10, release date: 2011-06-01, Last modification date: 2023-09-13) |
| Primary citation | Kiliszek, A.,Kierzek, R.,Krzyzosiak, W.J.,Rypniewski, W. Crystal structures of CGG RNA repeats with implications for fragile X-associated tremor ataxia syndrome. Nucleic Acids Res., 39:7308-7315, 2011 Cited by PubMed Abstract: The CGG repeats are present in the 5'-untranslated region (5'-UTR) of the fragile X mental retardation gene FMR1 and are associated with two diseases: fragile X-associated tremor ataxia syndrome (FXTAS) and fragile X syndrome (FXS). FXTAS occurs when the number of repeats is 55-200 and FXS develops when the number exceeds 200. FXTAS is an RNA-mediated disease in which the expanded CGG tracts form stable structures and sequester important RNA binding proteins. We obtained and analysed three crystal structures of double-helical CGG repeats involving unmodified and 8-Br modified guanosine residues. Despite the presence of the non-canonical base pairs, the helices retain an A-form. In the G-G pairs one guanosine is always in the syn conformation, the other is anti. There are two hydrogen bonds between the Watson-Crick edge of G(anti) and the Hoogsteen edge of G(syn): O6·N1H and N7·N2H. The G(syn)-G(anti) pair shows affinity for binding ions in the major groove. G(syn) causes local unwinding of the helix, compensated elsewhere along the duplex. CGG helical structures appear relatively stable compared with CAG and CUG tracts. This could be an important factor in the RNA's ligand binding affinity and specificity. PubMed: 21596781DOI: 10.1093/nar/gkr368 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.0531 Å) |
Structure validation
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