1G2E

CRYSTAL STRUCTURE OF HUD AND AU-RICH ELEMENT OF THE TUMOR NECROSIS FACTOR ALPHA RNA

1G2E の概要

• エントリーDOI: 10.2210/pdb1g2e/pdb
• 関連するPDBエントリー: 1FXL
• 分子名称: 5'-R(P*UP*AP*UP*UP*UP*AP*UP*UP*UP*A)-3', PARANEOPLASTIC ENCEPHALOMYELITIS ANTIGEN HUD (3 entities in total)
• 機能のキーワード: protein-rna complex, hud, au-rich element, tumor necrosis factor, transcription-rna complex, transcription/rna
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 21633.01

構造登録者

Wang, X.,Hall, T.M.T. (登録日: 2000-10-18, 公開日: 2001-02-05, 最終更新日: 2023-08-02)

主引用文献

Wang, X.,Tanaka Hall, T.M.
Structural basis for recognition of AU-rich element RNA by the HuD protein.
Nat.Struct.Biol., 8:141-145, 2001

PubMed Abstract: Hu proteins bind to adenosine-uridine (AU)-rich elements (AREs) in the 3' untranslated regions of many short-lived mRNAs, thereby stabilizing them. Here we report the crystal structures of the first two RNA recognition motif (RRM) domains of the HuD protein in complex with an 11-nucleotide fragment of a class I ARE (the c-fos ARE; to 1.8 A), and with an 11-nucleotide fragment of a class II ARE (the tumor necrosis factor alpha ARE; to 2.3 A). These structures reveal a consensus RNA recognition sequence that suggests a preference for pyrimidine-rich sequences and a requirement for a central uracil residue in the clustered AUUUA repeats found in class II AREs. Comparison to structures of other RRM domain-nucleic acid complexes reveals two base recognition pockets in all the structures that interact with bases using residues in conserved ribonucleoprotein motifs and at the C-terminal ends of RRM domains. Different conformations of nucleic acid can be bound by RRM domains by using different combinations of base recognition pockets and multiple RRM domains.

PubMed: 11175903
DOI: 10.1038/84131

実験手法

X-RAY DIFFRACTION (2.3 Å)