2OXQ
Structure of the UbcH5 :CHIP U-box complex
Summary for 2OXQ
| Entry DOI | 10.2210/pdb2oxq/pdb |
| Descriptor | Ubiquitin-conjugating enzyme E2D 1, STIP1 homology and U-Box containing protein 1, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | protein-protein complex, ligase |
| Biological source | Danio rerio (zebrafish) More |
| Total number of polymer chains | 4 |
| Total formula weight | 52338.12 |
| Authors | Xu, Z.,Nix, J.C.,Devlin, K.I.,Misra, S. (deposition date: 2007-02-20, release date: 2008-02-19, Last modification date: 2023-08-30) |
| Primary citation | Xu, Z.,Kohli, E.,Devlin, K.I.,Bold, M.,Nix, J.C.,Misra, S. Interactions between the quality control ubiquitin ligase CHIP and ubiquitin conjugating enzymes. Bmc Struct.Biol., 8:26-26, 2008 Cited by PubMed Abstract: Ubiquitin (E3) ligases interact with specific ubiquitin conjugating (E2) enzymes to ubiquitinate particular substrate proteins. As the combination of E2 and E3 dictates the type and biological consequence of ubiquitination, it is important to understand the basis of specificity in E2:E3 interactions. The E3 ligase CHIP interacts with Hsp70 and Hsp90 and ubiquitinates client proteins that are chaperoned by these heat shock proteins. CHIP interacts with two types of E2 enzymes, UbcH5 and Ubc13-Uev1a. It is unclear, however, why CHIP binds these E2 enzymes rather than others, and whether CHIP interacts preferentially with UbcH5 or Ubc13-Uev1a, which form different types of polyubiquitin chains. PubMed: 18485199DOI: 10.1186/1472-6807-8-26 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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