5MF9

Solution structure of the RBM5 OCRE domain in complex with polyproline SmN peptide.

5MF9 の概要

• エントリーDOI: 10.2210/pdb5mf9/pdb
• NMR情報: BMRB: 34067
• 分子名称: RNA-binding protein 5, Survival motor neuron protein (2 entities in total)
• 機能のキーワード: ocre, poly proline binding domain, smn, alternative splicing, splicing
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Nucleus : P52756; Nucleus, gem : Q16637
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 8573.16

構造登録者

Mourao, A.,Sattler, M.,Bonnal, S.,Komal, S.,Warner, L.,Bordonne, R.,Valcarcel, J. (登録日: 2016-11-17, 公開日: 2016-12-07, 最終更新日: 2024-05-15)

主引用文献

Mourao, A.,Bonnal, S.,Komal, S.,Warner, L.,Bordonne, R.,Valcarcel, J.,Sattler, M.
Structural basis for the recognition ofspliceosomal SmN B B proteins by theRBM5 OCRE domain in splicing regulation
Elife, 5:1-25, 2016

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: 27894420
DOI: 10.7554/eLife.14707

実験手法

SOLUTION NMR