2MKK

Structural model of tandem RRM domains of cytoplasmic polyadenylation element binding protein 1 (CPEB1) in complex with RNA

2MKK の概要

• エントリーDOI: 10.2210/pdb2mkk/pdb
• 関連するPDBエントリー: 2MKE 2MKH 2MKI 2MKJ
• NMR情報: BMRB: 19778
• 分子名称: Cytoplasmic polyadenylation element-binding protein 1, RNA (5'-R(*UP*UP*UP*UP*A)-3') (2 entities in total)
• 機能のキーワード: cpeb1, rna recognition motif (rrm), cytoplasmic polyadenylation, protein-rna interaction, translation regulation, translation regulator-rna complex, translation regulator/rna
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm, P-body: Q9BZB8
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 25439.49

構造登録者

Afroz, T.,Skrisovska, L.,Belloc, E.,Boixet, J.G.,Mendez, R.,Allain, F.H.-T. (登録日: 2014-02-07, 公開日: 2014-07-23, 最終更新日: 2024-05-01)

主引用文献

Afroz, T.,Skrisovska, L.,Belloc, E.,Guillen-Boixet, J.,Mendez, R.,Allain, F.H.-T.
A fly trap mechanism provides sequence-specific RNA recognition by CPEB proteins
Genes Dev., 28:1498-1514, 2014

PubMed Abstract: Cytoplasmic changes in polyA tail length is a key mechanism of translational control and is implicated in germline development, synaptic plasticity, cellular proliferation, senescence, and cancer progression. The presence of a U-rich cytoplasmic polyadenylation element (CPE) in the 3' untranslated regions (UTRs) of the responding mRNAs gives them the selectivity to be regulated by the CPE-binding (CPEB) family of proteins, which recognizes RNA via the tandem RNA recognition motifs (RRMs). Here we report the solution structures of the tandem RRMs of two human paralogs (CPEB1 and CPEB4) in their free and RNA-bound states. The structures reveal an unprecedented arrangement of RRMs in the free state that undergo an original closure motion upon RNA binding that ensures high fidelity. Structural and functional characterization of the ZZ domain (zinc-binding domain) of CPEB1 suggests a role in both protein-protein and protein-RNA interactions. Together with functional studies, the structures reveal how RNA binding by CPEB proteins leads to an optimal positioning of the N-terminal and ZZ domains at the 3' UTR, which favors the nucleation of the functional ribonucleoprotein complexes for translation regulation.

PubMed: 24990967
DOI: 10.1101/gad.241133.114

実験手法

SOLUTION NMR