4CQ1 の概要
| エントリーDOI | 10.2210/pdb4cq1/pdb |
| 分子名称 | POLYPYRIMIDINE TRACT-BINDING PROTEIN 2, ZINC ION, CHLORIDE ION, ... (4 entities in total) |
| 機能のキーワード | translation, rna binding protein, nptb, brptb |
| 由来する生物種 | HOMO SAPIENS (HUMAN) |
| 細胞内の位置 | Nucleus : Q9UKA9 |
| タンパク質・核酸の鎖数 | 8 |
| 化学式量合計 | 176661.11 |
| 構造登録者 | |
| 主引用文献 | Joshi, A.,Esteve, V.,Buckroyd, A.N.,Blatter, M.,Allain, F.H.-T.,Curry, S. Solution and Crystal Structures of a C Terminal Fragment of the Neuronal Isoform of the Polypyrimidine Tract Binding Protein (Nptb) Peerj, 2:E305-, 2014 Cited by PubMed Abstract: The eukaryotic polypyrimidine tract binding protein (PTB) serves primarily as a regulator of alternative splicing of messenger RNA, but is also co-opted to other roles such as RNA localisation and translation initiation from internal ribosome entry sites. The neuronal paralogue of PTB (nPTB) is 75% identical in amino acid sequence with PTB. Although the two proteins have broadly similar RNA binding specificities and effects on RNA splicing, differential expression of PTB and nPTB can lead to the generation of alternatively spliced mRNAs. RNA binding by PTB and nPTB is mediated by four RNA recognition motifs (RRMs). We present here the crystal and solution structures of the C-terminal domain of nPTB (nPTB34) which contains RRMs 3 and 4. As expected the structures are similar to each other and to the solution structure of the equivalent fragment from PTB (PTB34). The result confirms that, as found for PTB, RRMs 3 and 4 of nPTB interact with one another to form a stable unit that presents the RNA-binding surfaces of the component RRMs on opposite sides that face away from each other. The major differences between PTB34 and nPTB34 arise from amino acid side chain substitutions on the exposed β-sheet surfaces and adjoining loops of each RRM, which are likely to modulate interactions with RNA. PubMed: 24688880DOI: 10.7717/PEERJ.305 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.69 Å) |
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