2CJK
Structure of the RNA binding domain of Hrp1 in complex with RNA
2CJK の概要
エントリーDOI | 10.2210/pdb2cjk/pdb |
分子名称 | NUCLEAR POLYADENYLATED RNA-BINDING PROTEIN 4, 5'-R(*UP*AP*UP*AP*UP*AP*UP*AP)-3' (2 entities in total) |
機能のキーワード | hrp1, rna-binding, rna processing, mrna processing, nonsense-mediated mrna decay, cleavage, polyadenylation, nuclear protein, rna-binding protein, rna binding protein |
由来する生物種 | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) 詳細 |
細胞内の位置 | Cytoplasm: Q99383 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 21562.09 |
構造登録者 | |
主引用文献 | Perez-Canadillas, J.M. Grabbing the message: structural basis of mRNA 3'UTR recognition by Hrp1. EMBO J., 25:3167-3178, 2006 Cited by PubMed Abstract: The recognition of specific signals encoded within the 3'-untranslated region of the newly transcribed mRNA triggers the assembly of a multiprotein machine that modifies its 3'-end. Hrp1 recognises one of such signals, the so-called polyadenylation enhancement element (PEE), promoting the recruitment of other polyadenylation factors in yeast. The molecular bases of this interaction are revealed here by the solution structure of a complex between Hrp1 and an oligonucleotide mimicking the PEE. Six consecutive bases (AUAUAU) are specifically recognised by two RNA-binding domains arranged in tandem. Both protein and RNA undergo significant conformational changes upon complex formation with a concomitant large surface burial of RNA bases. Key aspects of RNA specificity can be explained by the presence of intermolecular aromatic-aromatic contacts and hydrogen bonds. Altogether, the Hrp1-PEE structure represents one of the first steps towards understanding of the assembly of the cleavage and polyadenylation machinery at the atomic level. PubMed: 16794580DOI: 10.1038/sj.emboj.7601190 主引用文献が同じPDBエントリー |
実験手法 | SOLUTION NMR |
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