2mb0 | pdb_00002mb0

Solution structure of hnRNP G RRM in complex with the RNA 5'-AUCAAA-3'

spinqualitylabelsall models 2mb0, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mb0 is a 2 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: RBMX, HNRPG, RBMXP1 (HUMAN) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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-beta1. 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-beta1 binding site. Finally, our data suggest that hnRNP G plays a major role in the recruitment of the Tra2-beta1/hnRNP G/SRSF9 trimeric complex to SMN2 exon 7. Characterization of the RNA recognition mode of hnRNP G extends its role in SMN2 splicing regulation.,Moursy A, Allain FH, Clery A Nucleic Acids Res. 2014 Apr 4. PMID:24692659 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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