1UOH

HUMAN GANKYRIN

1UOH の概要

• エントリーDOI: 10.2210/pdb1uoh/pdb
• 分子名称: 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 10 (2 entities in total)
• 機能のキーワード: oncoprotein, ankyrin repeat, 26s proteasome
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Cytoplasm: O75832
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24459.85

構造登録者

Krzywda, S.,Brzozowski, A.M.,Wilkinson, A.J. (登録日: 2003-09-17, 公開日: 2003-10-30, 最終更新日: 2023-12-13)

主引用文献

Krzywda, S.,Brzozowski, A.M.,Higashitsuji, H.,Fujita, J.,Welchman, R.,Dawson, S.,Mayer, R.J.,Wilkinson, A.J.
The Crystal Structure of Gankyrin, an Oncoprotein Found in Complexes with Cyclin-Dependent Kinase 4, a 19 S Proteasomal ATPase Regulator, and the Tumor Suppressors Rb and P53
J.Biol.Chem., 279:1541-, 2004

PubMed Abstract: Gankyrin is a 25-kDa hepatocellular carcinoma-associated protein that mediates protein-protein interactions in cell cycle control and protein degradation. It has been reported to form complexes with cyclin-dependent kinase 4, retinoblastoma protein, the S6b ATPase subunit of the 19 S regulator of the 26 S proteasome, and Mdm2, an E3 ubiquitin ligase involved in p53 degradation. It is the first protein described to bind both to the 26 S proteasome and to proteins in other complexes containing cyclin-dependent kinase(s) and p53 ubiquitylating activities, thus providing a mechanism for delivering cell cycle regulating machinery and ubiquitylated substrates to the proteasome for degradation. Gankyrin contains a 33-residue motif known as the ankyrin repeat that occurs five and a half to six times in the sequence. As a step toward understanding gankyrin interactions with its protein partners we have determined its three-dimensional crystal structure to 2.0-A resolution. It reveals that the entire 226-residue gankyrin polypeptide folds into seven ankyrin repeat elements. The ankyrin repeats, consisting of an antiparallel beta-hairpin followed by a perpendicularly oriented helix-loop-helix, pack side-by-side, creating an extended curved structure with a groove running across the long concave surface. Comparison with the structures of other ankyrin repeat proteins suggests that interactions with partner proteins are mediated by residues situated on this concave surface.

PubMed: 14573599
DOI: 10.1074/JBC.M310265200

実験手法

X-RAY DIFFRACTION (2 Å)