1IYF
Solution structure of ubiquitin-like domain of human parkin
Summary for 1IYF
| Entry DOI | 10.2210/pdb1iyf/pdb |
| NMR Information | BMRB: 5500 |
| Descriptor | parkin (1 entity in total) |
| Functional Keywords | ubiquitin fold, riken structural genomics/proteomics initiative, rsgi, structural genomics, ligase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm, cytosol: O60260 |
| Total number of polymer chains | 1 |
| Total formula weight | 9247.54 |
| Authors | Sakata, E.,Yamaguchi, Y.,Kurimoto, E.,Kikuchi, J.,Yokoyama, S.,Kawahara, H.,Yokosawa, H.,Hattori, N.,Mizuno, Y.,Tanaka, K.,Kato, K.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2002-08-13, release date: 2003-03-25, Last modification date: 2023-12-27) |
| Primary citation | Sakata, E.,Yamaguchi, Y.,Kurimoto, E.,Kikuchi, J.,Yokoyama, S.,Yamada, S.,Kawahara, H.,Yokosawa, H.,Hattori, N.,Mizuno, Y.,Tanaka, K.,Kato, K. Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin-like domain EMBO REP., 4:301-306, 2003 Cited by PubMed Abstract: Parkin, a product of the causative gene of autosomal-recessive juvenile parkinsonism (AR-JP), is a RING-type E3 ubiquitin ligase and has an amino-terminal ubiquitin-like (Ubl) domain. Although a single mutation that causes an Arg to Pro substitution at position 42 of the Ubl domain (the Arg 42 mutation) has been identified in AR-JP patients, the function of this domain is not clear. In this study, we determined the three-dimensional structure of the Ubl domain of parkin by NMR, in particular by extensive use of backbone (15)N-(1)H residual dipolar-coupling data. Inspection of chemical-shift-perturbation data showed that the parkin Ubl domain binds the Rpn10 subunit of 26S proteasomes via the region of parkin that includes position 42. Our findings suggest that the Arg 42 mutation induces a conformational change in the Rpn10-binding site of Ubl, resulting in impaired proteasomal binding of parkin, which could be the cause of AR-JP. PubMed: 12634850DOI: 10.1038/sj.embor.embor764 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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