4B6H

Structure of hDcp1a in complex with proline rich sequence of PNRC2

4B6H の概要

• エントリーDOI: 10.2210/pdb4b6h/pdb
• 分子名称: MRNA-DECAPPING ENZYME 1A, PROLINE-RICH NUCLEAR RECEPTOR COACTIVATOR 2 (3 entities in total)
• 機能のキーワード: hydrolase-peptide complex, decapping, hydrolase/peptide
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• 細胞内の位置: Cytoplasm, P-body: Q9NPI6; Nucleus: Q9NPJ4
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 61236.68

構造登録者

Lai, T.,Song, H. (登録日: 2012-08-13, 公開日: 2013-03-06, 最終更新日: 2024-05-08)

主引用文献

Lai, T.,Cho, H.,Liu, Z.,Bowler, M.W.,Piao, S.,Parker, R.,Kim, Y.K.,Song, H.
Structural Basis of the Pnrc2-Mediated Link between Mrna Surveillance and Decapping.
Structure, 20:2025-, 2012

PubMed Abstract: Nonsense-mediated mRNA decay (NMD) is an important mRNA surveillance system, and human PNRC2 protein mediates the link between mRNA surveillance and decapping. However, the mechanism by which PNRC2 interacts with the mRNA surveillance machinery and stimulates NMD is unknown. Here, we present the crystal structure of Dcp1a in complex with PNRC2. The proline-rich region of PNRC2 is bound to the EVH1 domain of Dcp1a, while its NR-box mediates the interaction with the hyperphosphorylated Upf1. The mode of PNRC2 interaction with Dcp1a is distinct from those observed in other EVH1/proline-rich ligands interactions. Disruption of the interaction of PNRC2 with Dcp1a abolishes its P-body localization and ability to promote mRNA degradation when tethered to mRNAs. PNRC2 acts in synergy with Dcp1a to stimulate the decapping activity of Dcp2 by bridging the interaction between Dcp1a and Dcp2, suggesting that PNRC2 is a decapping coactivator in addition to its adaptor role in NMD.

PubMed: 23085078
DOI: 10.1016/J.STR.2012.09.009

実験手法

X-RAY DIFFRACTION (2.6 Å)