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1D9A

SOLUTION STRUCTURE OF THE SECOND RNA-BINDING DOMAIN (RBD2) OF HU ANTIGEN C (HUC)

1D9A の概要
エントリーDOI10.2210/pdb1d9a/pdb
関連するPDBエントリー1D8Z
分子名称HU ANTIGEN C (1 entity in total)
機能のキーワードrna-binding domain, riken structural genomics/proteomics initiative, rsgi, structural genomics, rna binding protein
由来する生物種Mus musculus (house mouse)
タンパク質・核酸の鎖数1
化学式量合計9351.66
構造登録者
Inoue, M.,Muto, Y.,Sakamoto, H.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 1999-10-26, 公開日: 2000-04-07, 最終更新日: 2024-05-22)
主引用文献Inoue, M.,Muto, Y.,Sakamoto, H.,Yokoyama, S.
NMR studies on functional structures of the AU-rich element-binding domains of Hu antigen C.
Nucleic Acids Res., 28:1743-1750, 2000
Cited by
PubMed Abstract: Hu antigen C (HuC) has three RNA-binding domains (RBDs). The N-terminal two, RBD1 and RBD2, are linked in tandem and bind to the AU-rich elements (AREs) in the 3'-untranslated region of particular mRNAs. The solution structures of HuC RBD1 and RBD2 were determined by NMR methods. The HuC RBD1 and RBD2 structures are quite similar to those of Sxl RBD1 and RBD2, respectively. The individual RBDs of HuC, RBD1 and RBD2 in isolation can interact rather weakly with the minimal ARE motif, AUUUA, while the didomain fragment, RBD1-RBD2, of HuC binds more tightly to a longer ARE RNA, UAUUUAUUUU. Chemical shift perturbations by the longer RNA on HuC RBD1-RBD2 were mapped on and around the two beta-sheets and on the C-terminal region of RBD1. The HuC RBD1-RBD2 residues that exhibited significant chemical shift perturbations coincide with those conserved in Sxl RBD1-RBD2. These data indicate that the RNA-binding characteristics of the HuC and Sxl didomain fragments are similar, even though the target RNAs and the biological functions of the proteins are different.
PubMed: 10734193
DOI: 10.1093/nar/28.8.1743
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実験手法
SOLUTION NMR
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件を2025-12-31に公開中

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