6B3X
Crystal structure of CstF-50 in complex with CstF-77
6B3X の概要
| エントリーDOI | 10.2210/pdb6b3x/pdb |
| 分子名称 | Cleavage stimulation factor subunit 1, Cleavage stimulation factor subunit 3 (3 entities in total) |
| 機能のキーワード | wd40 fold, scaffold protein, gene regulation |
| 由来する生物種 | Homo sapiens (Human) 詳細 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 42696.01 |
| 構造登録者 | Yang, W.,Hsu, P.,Yang, F.,Song, J.E.,Varani, G. (登録日: 2017-09-25, 公開日: 2017-11-29, 最終更新日: 2024-04-03) |
| 主引用文献 | Yang, W.,Hsu, P.L.,Yang, F.,Song, J.E.,Varani, G. Reconstitution of the CstF complex unveils a regulatory role for CstF-50 in recognition of 3'-end processing signals. Nucleic Acids Res., 46:493-503, 2018 Cited by PubMed Abstract: Cleavage stimulation factor (CstF) is a highly conserved protein complex composed of three subunits that recognizes G/U-rich sequences downstream of the polyadenylation signal of eukaryotic mRNAs. While CstF has been identified over 25 years ago, the architecture and contribution of each subunit to RNA recognition have not been fully understood. In this study, we provide a structural basis for the recruitment of CstF-50 to CstF via interaction with CstF-77 and establish that the hexameric assembly of CstF creates a high affinity platform to target various G/U-rich sequences. We further demonstrate that CstF-77 boosts the affinity of the CstF-64 RRM to the RNA targets and CstF-50 fine tunes the ability of the complex to recognize G/U sequences of certain lengths and content. PubMed: 29186539DOI: 10.1093/nar/gkx1177 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.3 Å) |
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