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2DVW

Structure of the Oncoprotein Gankyrin in Complex with S6 ATPase of the 26S Proteasome

Summary for 2DVW
Entry DOI10.2210/pdb2dvw/pdb
Descriptor26S proteasome non-ATPase regulatory subunit 10, 26S protease regulatory subunit 6B (3 entities in total)
Functional Keywordsankyrin 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
Biological sourceMus musculus (house mouse)
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Cellular locationCytoplasm (By similarity): Q9Z2X2
Cytoplasm: P43686
Total number of polymer chains2
Total formula weight34880.71
Authors
Yokoyama, S.,Padmanabhan, B.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2006-08-01, release date: 2007-03-13, Last modification date: 2023-10-25)
Primary citationNakamura, 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: 17292836
DOI: 10.1016/j.str.2006.11.015
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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