2MB0
Solution structure of hnRNP G RRM in complex with the RNA 5'-AUCAAA-3'
Summary for 2MB0
| Entry DOI | 10.2210/pdb2mb0/pdb |
| NMR Information | BMRB: 19382 |
| Descriptor | RNA-binding motif protein, X chromosome, RNA_(5'-R(*AP*UP*CP*AP*AP*A)-3') (2 entities in total) |
| Functional Keywords | hnrnp g, splicing, rrm, smn, sma, splicing-rna complex, splicing/rna |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: P38159 |
| Total number of polymer chains | 2 |
| Total formula weight | 12297.03 |
| Authors | Moursy, A.,Allain, F.H.-T.,Clery, A. (deposition date: 2013-07-22, release date: 2014-04-09, Last modification date: 2024-05-01) |
| Primary citation | Moursy, A.,Allain, F.H.,Clery, A. Characterization of the RNA recognition mode of hnRNP G extends its role in SMN2 splicing regulation. Nucleic Acids Res., 42:6659-6672, 2014 Cited by PubMed Abstract: Regulation of SMN2 exon 7 splicing is crucial for the production of active SMN protein and the survival of Spinal Muscular Atrophy (SMA) patients. One of the most efficient activators of exon 7 inclusion is hnRNP G, which is recruited to the exon by Tra2-β1. We report that in addition to the C-terminal region of hnRNP G, the RNA Recognition Motif (RRM) and the middle part of the protein containing the Arg-Gly-Gly (RGG) box are important for this function. To better understand the mode of action of hnRNP G in this context we determined the structure of its RRM bound to an SMN2 derived RNA. The RRM interacts with a 5'-AAN-3' motif and specifically recognizes the two consecutive adenines. By testing the effect of mutations in hnRNP G RRM and in its putative binding sites on the splicing of SMN2 exon 7, we show that it specifically binds to exon 7. This interaction is required for hnRNP G splicing activity and we propose its recruitment to a polyA tract located upstream of the Tra2-β1 binding site. Finally, our data suggest that hnRNP G plays a major role in the recruitment of the Tra2-β1/hnRNP G/SRSF9 trimeric complex to SMN2 exon 7. PubMed: 24692659DOI: 10.1093/nar/gku244 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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