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3r1c

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3r1c, resolution 2.05Å ()
Sites: , , , , , and
Ligands:
Related: 3r1d, 3r1e


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of GCGGCGGC duplex

Publication Abstract from PubMed

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.

Crystal structures of CGG RNA repeats with implications for fragile X-associated tremor ataxia syndrome., Kiliszek A, Kierzek R, Krzyzosiak WJ, Rypniewski W, Nucleic Acids Res. 2011 May 19. PMID:21596781

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

3r1c is a 36 chain structure. Full crystallographic information is available from OCA.

Reference

  • Kiliszek A, Kierzek R, Krzyzosiak WJ, Rypniewski W. Crystal structures of CGG RNA repeats with implications for fragile X-associated tremor ataxia syndrome. Nucleic Acids Res. 2011 May 19. PMID:21596781 doi:10.1093/nar/gkr368

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