4ZLR

Structure of the Brat-NHL domain bound to consensus RNA motif

4ZLR の概要

• エントリーDOI: 10.2210/pdb4zlr/pdb
• 分子名称: Brain tumor protein, RNA (5'-R(*UP*UP*GP*UP*UP*GP*UP*UP*UP*UP*UP*UP*UP*U)-3'), 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL, ... (7 entities in total)
• 機能のキーワード: nhl-domain, beta-propeller, rna binding, translational repressor, translation
• 由来する生物種: Drosophila melanogaster (Fruit fly); 詳細
• 細胞内の位置: Cytoplasm : Q8MQJ9
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 70209.95

構造登録者

Jakob, L.,Treiber, N.,Treiber, T.,Stotz, M.,Loedige, I.,Meister, G. (登録日: 2015-05-01, 公開日: 2015-11-11, 最終更新日: 2024-01-10)

主引用文献

Loedige, I.,Jakob, L.,Treiber, T.,Ray, D.,Stotz, M.,Treiber, N.,Hennig, J.,Cook, K.B.,Morris, Q.,Hughes, T.R.,Engelmann, J.C.,Krahn, M.P.,Meister, G.
The Crystal Structure of the NHL Domain in Complex with RNA Reveals the Molecular Basis of Drosophila Brain-Tumor-Mediated Gene Regulation.
Cell Rep, 13:1206-1220, 2015

PubMed Abstract: TRIM-NHL proteins are conserved among metazoans and control cell fate decisions in various stem cell linages. The Drosophila TRIM-NHL protein Brain tumor (Brat) directs differentiation of neuronal stem cells by suppressing self-renewal factors. Brat is an RNA-binding protein and functions as a translational repressor. However, it is unknown which RNAs Brat regulates and how RNA-binding specificity is achieved. Using RNA immunoprecipitation and RNAcompete, we identify Brat-bound mRNAs in Drosophila embryos and define consensus binding motifs for Brat as well as a number of additional TRIM-NHL proteins, indicating that TRIM-NHL proteins are conserved, sequence-specific RNA-binding proteins. We demonstrate that Brat-mediated repression and direct RNA-binding depend on the identified motif and show that binding of the localization factor Miranda to the Brat-NHL domain inhibits Brat activity. Finally, to unravel the sequence specificity of the NHL domain, we crystallize the Brat-NHL domain in complex with RNA and present a high-resolution protein-RNA structure of this fold.

PubMed: 26527002
DOI: 10.1016/j.celrep.2015.09.068

実験手法

X-RAY DIFFRACTION (2.3 Å)