2I2Y

Solution structure of the RRM of SRp20 bound to the RNA CAUC

2I2Y の概要

• エントリーDOI: 10.2210/pdb2i2y/pdb
• 分子名称: (5'-R(*CP*AP*UP*C)-3'), Fusion protein consists of immunoglobulin G-Binding Protein G and Splicing factor, arginine/serine-rich 3 (2 entities in total)
• 機能のキーワード: protein-rna complex rrm alpha-beta sandwich beta1-alpha1-beta2-beta3-alpha2-beta4, rna binding protein-chimera-rna complex, rna binding protein/chimera/rna
• 由来する生物種: Streptococcus sp. 'group G', Homo sapiens (, human)
• 細胞内の位置: Nucleus: P84103
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18061.46

構造登録者

Hargous, Y.F.,Allain, F.H. (登録日: 2006-08-17, 公開日: 2006-12-12, 最終更新日: 2024-05-29)

主引用文献

Hargous, Y.,Hautbergue, G.M.,Tintaru, A.M.,Skrisovska, L.,Golovanov, A.P.,Stevenin, J.,Lian, L.Y.,Wilson, S.A.,Allain, F.H.
Molecular basis of RNA recognition and TAP binding by the SR proteins SRp20 and 9G8.
Embo J., 25:5126-5137, 2006

PubMed Abstract: The sequence-specific RNA-binding proteins SRp20 and 9G8 are the smallest members of the serine- and arginine-rich (SR) protein family, well known for their role in splicing. They also play a role in mRNA export, in particular of histone mRNAs. We present the solution structures of the free 9G8 and SRp20 RNA recognition motifs (RRMs) and of SRp20 RRM in complex with the RNA sequence 5'CAUC3'. The SRp20-RNA structure reveals that although all 4 nt are contacted by the RRM, only the 5' cytosine is primarily recognized in a specific way. This might explain the numerous consensus sequences found by SELEX (systematic evolution of ligands by exponential enrichment) for the RRM of 9G8 and SRp20. Furthermore, we identify a short arginine-rich peptide adjacent to the SRp20 and 9G8 RRMs, which does not contact RNA but is necessary and sufficient for interaction with the export factor Tip-associated protein (TAP). Together, these results provide a molecular description for mRNA and TAP recognition by SRp20 and 9G8.

PubMed: 17036044
DOI: 10.1038/sj.emboj.7601385

実験手法

SOLUTION NMR