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• W2137474088 abstract "G-quadruplexes form from G rich sequences and have previously been suggested to be involved in various aspects of mRNA metabolism. The structure of an RNA quadruplex-duplex junction in complex with an Arg-Gly-rich peptide from Fragile X mental retardation protein (FMRP) now reveals an unprecedented RNA scaffold and principles underlying its specific recognition. We have determined the solution structure of the complex between an arginine-glycine-rich RGG peptide from the human fragile X mental retardation protein (FMRP) and an in vitro–selected guanine-rich (G-rich) sc1 RNA. The bound RNA forms a newly discovered G-quadruplex separated from the flanking duplex stem by a mixed junctional tetrad. The RGG peptide is positioned along the major groove of the RNA duplex, with the G-quadruplex forcing a sharp turn of R10GGGGR15 at the duplex-quadruplex junction. Arg10 and Arg15 form cross-strand specificity–determining intermolecular hydrogen bonds with the major-groove edges of guanines of adjacent Watson-Crick G•C pairs. Filter-binding assays on RNA and peptide mutations identify and validate contributions of peptide-RNA intermolecular contacts and shape complementarity to molecular recognition. These findings on FMRP RGG domain recognition by a combination of G-quadruplex and surrounding RNA sequences have implications for the recognition of other genomic G-rich RNAs." @default.
• W2137474088 created "2016-06-24" @default.
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• W2137474088 date "2011-06-05" @default.
• W2137474088 modified "2023-10-18" @default.
• W2137474088 title "Structure-function studies of FMRP RGG peptide recognition of an RNA duplex-quadruplex junction" @default.
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• W2137474088 doi "https://doi.org/10.1038/nsmb.2064" @default.
• W2137474088 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3130835" @default.
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• W2137474088 hasPublicationYear "2011" @default.
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