2RQC

Solution Structure of RNA-binding domain 3 of CUGBP1 in complex with RNA (UG)3

Summary for 2RQC

• Entry DOI: 10.2210/pdb2rqc/pdb
• Related: 2CPZ
• Descriptor: CUG-BP- and ETR-3-like factor 1, 5'-R(*UP*GP*UP*GP*UP*G)-3' (2 entities in total)
• Functional Keywords: rrm domain, rbd, protein-rna complex, transcription-rna complex, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, activator, alternative splicing, cytoplasm, mrna processing, nucleus, phosphoprotein, rna-binding, transcription/rna
• Biological source: Homo sapiens (Human); More
• Cellular location: Nucleus: Q92879
• Total number of polymer chains: 2
• Total formula weight: 14173.93

Authors

Tsuda, K.,Kuwasako, K.,Takahashi, M.,Someya, T.,Muto, Y.,Inoue, M.,Kigawa, T.,Terada, T.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2009-04-09, release date: 2009-08-04, Last modification date: 2024-05-29)

Primary citation

Tsuda, K.,Kuwasako, K.,Takahashi, M.,Someya, T.,Inoue, M.,Terada, T.,Kobayashi, N.,Shirouzu, M.,Kigawa, T.,Tanaka, A.,Sugano, S.,Guntert, P.,Muto, Y.,Yokoyama, S.
Structural basis for the sequence-specific RNA-recognition mechanism of human CUG-BP1 RRM3
Nucleic Acids Res., 37:5151-5166, 2009

PubMed Abstract: The CUG-binding protein 1 (CUG-BP1) is a member of the CUG-BP1 and ETR-like factors (CELF) family or the Bruno-like family and is involved in the control of splicing, translation and mRNA degradation. Several target RNA sequences of CUG-BP1 have been predicted, such as the CUG triplet repeat, the GU-rich sequences and the AU-rich element of nuclear pre-mRNAs and/or cytoplasmic mRNA. CUG-BP1 has three RNA-recognition motifs (RRMs), among which the third RRM (RRM3) can bind to the target RNAs on its own. In this study, we solved the solution structure of the CUG-BP1 RRM3 by hetero-nuclear NMR spectroscopy. The CUG-BP1 RRM3 exhibited a noncanonical RRM fold, with the four-stranded beta-sheet surface tightly associated with the N-terminal extension. Furthermore, we determined the solution structure of the CUG-BP1 RRM3 in the complex with (UG)(3) RNA, and discovered that the UGU trinucleotide is specifically recognized through extensive stacking interactions and hydrogen bonds within the pocket formed by the beta-sheet surface and the N-terminal extension. This study revealed the unique mechanism that enables the CUG-BP1 RRM3 to discriminate the short RNA segment from other sequences, thus providing the molecular basis for the comprehension of the role of the RRM3s in the CELF/Bruno-like family.

PubMed: 19553194
DOI: 10.1093/nar/gkp546

Experimental method

SOLUTION NMR