2LA5
RNA Duplex-Quadruplex Junction Complex with FMRP RGG peptide
Summary for 2LA5
| Entry DOI | 10.2210/pdb2la5/pdb |
| NMR Information | BMRB: 17504 |
| Descriptor | RNA (36-MER), Fragile X mental retardation 1 protein (2 entities in total) |
| Functional Keywords | rna binding protein-rna complex, rna binding protein/rna |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: Q06787 |
| Total number of polymer chains | 2 |
| Total formula weight | 13562.95 |
| Authors | Phan, A.,Kuryavyi, V.,Darnell, J.,Serganov, A.,Majumdar, A.,Ilin, S.,Darnell, R.,Patel, D. (deposition date: 2011-03-03, release date: 2011-06-08, Last modification date: 2024-05-01) |
| Primary citation | Phan, A.T.,Kuryavyi, V.,Darnell, J.C.,Serganov, A.,Majumdar, A.,Ilin, S.,Raslin, T.,Polonskaia, A.,Chen, C.,Clain, D.,Darnell, R.B.,Patel, D.J. Structure-function studies of FMRP RGG peptide recognition of an RNA duplex-quadruplex junction. Nat.Struct.Mol.Biol., 18:796-804, 2011 Cited by PubMed Abstract: 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 R(10)GGGGR(15) 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. PubMed: 21642970DOI: 10.1038/nsmb.2064 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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