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2RQ4

Refinement of RNA binding domain 3 in CUG triplet repeat RNA-binding protein 1

2RQ4 の概要
エントリーDOI10.2210/pdb2rq4/pdb
関連するPDBエントリー2CPZ
分子名称CUG-BP- and ETR-3-like factor 1 (1 entity in total)
機能のキーワードrrm domain, rbd, activator, alternative splicing, cytoplasm, mrna processing, nucleus, phosphoprotein, rna-binding, transcription, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi
由来する生物種Homo sapiens (human)
細胞内の位置Nucleus: Q92879
タンパク質・核酸の鎖数1
化学式量合計12264.78
構造登録者
主引用文献Tsuda, K.,Kuwasako, K.,Takahashi, M.,Someya, T.,Inoue, M.,Terada, T.,Kobayashi, N.,Shirouzu, M.,Kigawa, T.,Tanaka, A.,Sugano, S.,Guntert, P.,Muto, Y.,Yokoyama, S.
Structural basis for the sequence-specific RNA-recognition mechanism of human CUG-BP1 RRM3
Nucleic Acids Res., 2009
Cited by
PubMed Abstract: The CUG-binding protein 1 (CUG-BP1) is a member of the CUG-BP1 and ETR-like factors (CELF) family or the Bruno-like family and is involved in the control of splicing, translation and mRNA degradation. Several target RNA sequences of CUG-BP1 have been predicted, such as the CUG triplet repeat, the GU-rich sequences and the AU-rich element of nuclear pre-mRNAs and/or cytoplasmic mRNA. CUG-BP1 has three RNA-recognition motifs (RRMs), among which the third RRM (RRM3) can bind to the target RNAs on its own. In this study, we solved the solution structure of the CUG-BP1 RRM3 by hetero-nuclear NMR spectroscopy. The CUG-BP1 RRM3 exhibited a noncanonical RRM fold, with the four-stranded beta-sheet surface tightly associated with the N-terminal extension. Furthermore, we determined the solution structure of the CUG-BP1 RRM3 in the complex with (UG)(3) RNA, and discovered that the UGU trinucleotide is specifically recognized through extensive stacking interactions and hydrogen bonds within the pocket formed by the beta-sheet surface and the N-terminal extension. This study revealed the unique mechanism that enables the CUG-BP1 RRM3 to discriminate the short RNA segment from other sequences, thus providing the molecular basis for the comprehension of the role of the RRM3s in the CELF/Bruno-like family.
PubMed: 19553194
DOI: 10.1093/nar/gkp546
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2rq4
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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