5MFY
RBM5 OCRE domain
Summary for 5MFY
| Entry DOI | 10.2210/pdb5mfy/pdb |
| NMR Information | BMRB: 34068 |
| Descriptor | RNA-binding protein 5 (1 entity in total) |
| Functional Keywords | splicing, ocre |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 7436.78 |
| Authors | Warner, L.R.,Mourao, A.,Soni, K.,Sattler, M. (deposition date: 2016-11-19, release date: 2016-12-07, Last modification date: 2024-06-19) |
| Primary citation | Mourao, A.,Bonnal, S.,Soni, K.,Warner, L.,Bordonne, R.,Valcarcel, J.,Sattler, M. Structural basis for the recognition of spliceosomal SmN/B/B' proteins by the RBM5 OCRE domain in splicing regulation. Elife, 5:-, 2016 Cited by PubMed Abstract: The multi-domain splicing factor RBM5 regulates the balance between antagonistic isoforms of the apoptosis-control genes , and . An OCRE (OCtamer REpeat of aromatic residues) domain found in RBM5 is important for alternative splicing regulation and mediates interactions with components of the U4/U6.U5 tri-snRNP. We show that the RBM5 OCRE domain adopts a unique β-sheet fold. NMR and biochemical experiments demonstrate that the OCRE domain directly binds to the proline-rich C-terminal tail of the essential snRNP core proteins SmN/B/B'. The NMR structure of an OCRE-SmN peptide complex reveals a specific recognition of poly-proline helical motifs in SmN/B/B'. Mutation of conserved aromatic residues impairs binding to the Sm proteins and compromises RBM5-mediated alternative splicing regulation of FAS/CD95. Thus, RBM5 OCRE represents a poly-proline recognition domain that mediates critical interactions with the C-terminal tail of the spliceosomal SmN/B/B' proteins in alternative splicing regulation. PubMed: 27894420DOI: 10.7554/eLife.14707 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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