1G2E

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

Summary for 1G2E

• Entry DOI: 10.2210/pdb1g2e/pdb
• Related: 1FXL
• Descriptor: 5'-R(P*UP*AP*UP*UP*UP*AP*UP*UP*UP*A)-3', PARANEOPLASTIC ENCEPHALOMYELITIS ANTIGEN HUD (3 entities in total)
• Functional Keywords: protein-rna complex, hud, au-rich element, tumor necrosis factor, transcription-rna complex, transcription/rna
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 21633.01

Authors

Wang, X.,Hall, T.M.T. (deposition date: 2000-10-18, release date: 2001-02-05, Last modification date: 2023-08-02)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.3 Å)