5MFY: RBM5 OCRE domain

Citation:
Abstract
The multi-domain splicing factor RBM5 regulates the balance between antagonistic isoforms of the apoptosis-control genes FAS/CD95, Caspase-2 and AID. 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 beta-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 in vitro 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 FAS/CD95 alternative splicing regulation.
PDB ID: 5MFYDownload
MMDB ID: 145514
PDB Deposition Date: 2016/11/19
Updated in MMDB: 2016/12
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 5MFY: monomeric; determined by author and by software (PISA)
Molecular Components in 5MFY
Label Count Molecule
Protein (1 molecule)
1
RNA-binding Protein 5(Gene symbol: RBM5)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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