1UOH

HUMAN GANKYRIN

Summary for 1UOH

• Entry DOI: 10.2210/pdb1uoh/pdb
• Descriptor: 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 10 (2 entities in total)
• Functional Keywords: oncoprotein, ankyrin repeat, 26s proteasome
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm: O75832
• Total number of polymer chains: 1
• Total formula weight: 24459.85

Authors

Krzywda, S.,Brzozowski, A.M.,Wilkinson, A.J. (deposition date: 2003-09-17, release date: 2003-10-30, Last modification date: 2023-12-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2 Å)