2DVW
Structure of the Oncoprotein Gankyrin in Complex with S6 ATPase of the 26S Proteasome
2DVW の概要
エントリーDOI | 10.2210/pdb2dvw/pdb |
分子名称 | 26S proteasome non-ATPase regulatory subunit 10, 26S protease regulatory subunit 6B (3 entities in total) |
機能のキーワード | ankyrin repeats, a-helical domain, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, cell cycle-protein-binding complex, cell cycle/protein-binding |
由来する生物種 | Mus musculus (house mouse) 詳細 |
細胞内の位置 | Cytoplasm (By similarity): Q9Z2X2 Cytoplasm: P43686 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 34880.71 |
構造登録者 | Yokoyama, S.,Padmanabhan, B.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2006-08-01, 公開日: 2007-03-13, 最終更新日: 2023-10-25) |
主引用文献 | Nakamura, Y.,Nakano, K.,Umehara, T.,Kimura, M.,Hayashizaki, Y.,Tanaka, A.,Horikoshi, M.,Padmanabhan, B.,Yokoyama, S. Structure of the Oncoprotein Gankyrin in Complex with S6 ATPase of the 26S Proteasome Structure, 15:179-189, 2007 Cited by PubMed Abstract: Gankyrin is an oncoprotein commonly overexpressed in most hepatocellular carcinomas. Gankyrin interacts with S6 ATPase of the 19S regulatory particle of the 26S proteasome and enhances the degradation of the tumor suppressors pRb and p53. Here, we report the structure of gankyrin in complex with the C-terminal domain of S6 ATPase. Almost all of the seven ankyrin repeats of gankyrin interact, through its concave region, with the C-terminal domain of S6 ATPase. The intermolecular interactions occur through the complementary charged residues between gankyrin and S6 ATPase. Biochemical studies based on the structure of the complex revealed that gankyrin interacts with pRb in both the presence and absence of S6 ATPase; however, the E182 residue in gankyrin is essential for the pRb interaction. These results provide a structural basis for the involvement of gankyrin in the pRb degradation pathway, through its association with S6 ATPase of the 26S proteasome. PubMed: 17292836DOI: 10.1016/j.str.2006.11.015 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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