2RNE

Solution structure of the second RNA recognition motif (RRM) of TIA-1

2RNE の概要

• エントリーDOI: 10.2210/pdb2rne/pdb
• NMR情報: BMRB: 11370,11371,11372,11373,11374,11375,11376
• 分子名称: Tia1 protein (1 entity in total)
• 機能のキーワード: rrm domain, rna binding protein
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12432.72

構造登録者

Takahashi, M.,Kuwasako, K.,Abe, C.,Tsuda, K.,Inoue, M.,Terada, T.,Shirouzu, M.,Kobayashi, N.,Kigawa, T.,Taguchi, S.,Guntert, P.,Hayashizaki, Y.,Tanaka, A.,Muto, Y.,Yokoyama, S. (登録日: 2007-12-19, 公開日: 2008-11-04, 最終更新日: 2024-05-29)

主引用文献

Kuwasako, K.,Takahashi, M.,Tochio, N.,Abe, C.,Tsuda, K.,Inoue, M.,Terada, T.,Shirouzu, M.,Kobayashi, N.,Kigawa, T.,Taguchi, S.,Tanaka, A.,Hayashizaki, Y.,Guntert, P.,Muto, Y.,Yokoyama, S.
Solution structure of the second RNA recognition motif (RRM) domain of murine T cell intracellular antigen-1 (TIA-1) and its RNA recognition mode
Biochemistry, 47:6437-6450, 2008

PubMed Abstract: T cell intracellular antigen-1 (TIA-1), an apoptosis promoting factor, functions as a splicing regulator for the Fas pre-mRNA. TIA-1 possesses three RNA recognition motifs (RRMs) and a glutamine-rich domain. The second RRM (RRM2) is necessary and sufficient for tight, sequence-specific binding to the uridine-rich sequences buried around the 5' splice sites. In the present study, we solved the solution structure of the murine TIA-1 RRM2 by heteronuclear-nuclear magnetic resonance spectroscopy. The TIA-1 RRM2 adopts the RRM fold (betaalphabetabetaalphabeta) and possesses an extra beta-strand between beta2 and beta3, which forms an additional beta-sheet with the C-terminal part of beta2. We refer to this structure as the beta2-beta2' beta-loop. Interestingly, this characteristic beta-loop structure is conserved among a number of RRMs, including the U2AF65 RRM2 and the Sex-lethal RRM1 and RRM2, which also bind to uridine-rich RNAs. Furthermore, we identified a new sequence motif in the beta2-beta2' beta-loop, the DxxT motif. Chemical shift perturbation analyses of both the main and side chains upon binding to the uridine pentamer RNA revealed that most of the beta-sheet surface, including the beta2-beta2' beta-loop, is involved in the RNA binding. An investigation of the chemical shift perturbation revealed similarity in the RNA recognition modes between the TIA-1 and U2AF65 RRMs.

PubMed: 18500819
DOI: 10.1021/bi7024723

実験手法

SOLUTION NMR