5J28
Ki67-PP1g (protein phosphatase 1, gamma isoform) holoenzyme complex
5J28 の概要
| エントリーDOI | 10.2210/pdb5j28/pdb |
| 関連するPDBエントリー | 5INB 5IOH |
| 分子名称 | Serine/threonine-protein phosphatase PP1-gamma catalytic subunit, Antigen KI-67, MALONATE ION, ... (5 entities in total) |
| 機能のキーワード | pp1 gamma; repoman, ki-67; phosphatase, hydrolase-protein binding complex, hydrolase/protein binding |
| 由来する生物種 | Homo sapiens (Human) 詳細 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 80689.84 |
| 構造登録者 | |
| 主引用文献 | Kumar, G.S.,Gokhan, E.,De Munter, S.,Bollen, M.,Vagnarelli, P.,Peti, W.,Page, R. The Ki-67 and RepoMan mitotic phosphatases assemble via an identical, yet novel mechanism. Elife, 5:-, 2016 Cited by PubMed Abstract: Ki-67 and RepoMan have key roles during mitotic exit. Previously, we showed that Ki-67 organizes the mitotic chromosome periphery and recruits protein phosphatase 1 (PP1) to chromatin at anaphase onset, in a similar manner as RepoMan (Booth et al., 2014). Here we show how Ki-67 and RepoMan form mitotic exit phosphatases by recruiting PP1, how they distinguish between distinct PP1 isoforms and how the assembly of these two holoenzymes are dynamically regulated by Aurora B kinase during mitosis. Unexpectedly, our data also reveal that Ki-67 and RepoMan bind PP1 using an identical, yet novel mechanism, interacting with a PP1 pocket that is engaged only by these two PP1 regulators. These findings not only show how two distinct mitotic exit phosphatases are recruited to their substrates, but also provide immediate opportunities for the design of novel cancer therapeutics that selectively target the Ki-67:PP1 and RepoMan:PP1 holoenzymes. PubMed: 27572260DOI: 10.7554/eLife.16539 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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