4P6Q
The crystal structure of the Split End protein SHARP adds a new layer of complexity to proteins containing RNA Recognition Motifs
4P6Q の概要
エントリーDOI | 10.2210/pdb4p6q/pdb |
分子名称 | Msx2-interacting protein, SULFATE ION (3 entities in total) |
機能のキーワード | rna-recognition motif, spen protein, steroid rna activator, transcriptional regulation, transcription |
由来する生物種 | Homo sapiens (Human) |
細胞内の位置 | Nucleus : Q96T58 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 33152.79 |
構造登録者 | Arieti, F.,Gabus, C.,Tambalo, M.,Huet, T.,Round, A.,Thore, S. (登録日: 2014-03-25, 公開日: 2014-05-14, 最終更新日: 2023-12-20) |
主引用文献 | Arieti, F.,Gabus, C.,Tambalo, M.,Huet, T.,Round, A.,Thore, S. The crystal structure of the Split End protein SHARP adds a new layer of complexity to proteins containing RNA recognition motifs. Nucleic Acids Res., 42:6742-, 2014 Cited by PubMed Abstract: The Split Ends (SPEN) protein was originally discovered in Drosophila in the late 1990s. Since then, homologous proteins have been identified in eukaryotic species ranging from plants to humans. Every family member contains three predicted RNA recognition motifs (RRMs) in the N-terminal region of the protein. We have determined the crystal structure of the region of the human SPEN homolog that contains these RRMs-the SMRT/HDAC1 Associated Repressor Protein (SHARP), at 2.0 Å resolution. SHARP is a co-regulator of the nuclear receptors. We demonstrate that two of the three RRMs, namely RRM3 and RRM4, interact via a highly conserved interface. Furthermore, we show that the RRM3-RRM4 block is the main platform mediating the stable association with the H12-H13 substructure found in the steroid receptor RNA activator (SRA), a long, non-coding RNA previously shown to play a crucial role in nuclear receptor transcriptional regulation. We determine that SHARP association with SRA relies on both single- and double-stranded RNA sequences. The crystal structure of the SHARP-RRM fragment, together with the associated RNA-binding studies, extend the repertoire of nucleic acid binding properties of RRM domains suggesting a new hypothesis for a better understanding of SPEN protein functions. PubMed: 24748666DOI: 10.1093/nar/gku277 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2 Å) |
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