2LYD

The solution structure of the Dm DCP1 EVH1 domain in complex with the XRN1 DBM peptide

2LYD の概要

• エントリーDOI: 10.2210/pdb2lyd/pdb
• NMR情報: BMRB: 18720
• 分子名称: Decapping protein 1, Pacman protein (2 entities in total)
• 機能のキーワード: dcp1, xrn1, transcription-protein binding complex, transcription/protein binding
• 由来する生物種: Drosophila melanogaster (Fruit fly); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19830.27

構造登録者

Truffault, V. (登録日: 2012-09-17, 公開日: 2012-10-17, 最終更新日: 2024-05-01)

主引用文献

Braun, J.E.,Truffault, V.,Boland, A.,Huntzinger, E.,Chang, C.T.,Haas, G.,Weichenrieder, O.,Coles, M.,Izaurralde, E.
A direct interaction between DCP1 and XRN1 couples mRNA decapping to 5' exonucleolytic degradation.
Nat.Struct.Mol.Biol., 19:1324-1331, 2012

PubMed Abstract: The removal of the mRNA 5' cap structure by the decapping enzyme DCP2 leads to rapid 5'→3' mRNA degradation by XRN1, suggesting that the two processes are coordinated, but the coupling mechanism is unknown. DCP2 associates with the decapping activators EDC4 and DCP1. Here we show that XRN1 directly interacts with EDC4 and DCP1 in human and Drosophila melanogaster cells, respectively. In D. melanogaster cells, this interaction is mediated by the DCP1 EVH1 domain and a DCP1-binding motif (DBM) in the XRN1 C-terminal region. The NMR structure of the DCP1 EVH1 domain bound to the DBM reveals that the peptide docks at a conserved aromatic cleft, which is used by EVH1 domains to recognize proline-rich ligands. Our findings reveal a role for XRN1 in decapping and provide a molecular basis for the coupling of decapping to 5'→3' mRNA degradation.

PubMed: 23142987
DOI: 10.1038/nsmb.2413

実験手法

SOLUTION NMR