1P98
High-resolution NMR structure of the Ubl-domain of HHR23A
Summary for 1P98
| Entry DOI | 10.2210/pdb1p98/pdb |
| Related | 1DV0 1F4I 1IFY 1P9C 1P9D |
| Descriptor | UV excision repair protein RAD23 homolog A (1 entity in total) |
| Functional Keywords | ubiquitin-like domain, replication |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: P54725 |
| Total number of polymer chains | 1 |
| Total formula weight | 8953.53 |
| Authors | Mueller, T.D.,Feigon, J. (deposition date: 2003-05-09, release date: 2003-10-07, Last modification date: 2024-05-22) |
| Primary citation | Mueller, T.D.,Feigon, J. Structural determinants for the binding of ubiquitin-like domains to the proteasome. Embo J., 22:4634-4645, 2003 Cited by PubMed Abstract: HHR23A, a protein implicated in nucleotide excision repair, belongs to a class of proteins containing both a ubiquitin-like (Ubl) domain and one or more ubiquitin-associated (UBA) domains, suggesting a role in the ubiquitin-proteasome pathway as well. The Ubl domain binds with high affinity to the second ubiquitin-interacting motif (UIM) of the S5a subunit of the proteasome. Here we present the solution structures of the HHR23A Ubl domain, the second UIM of S5a (UIM-2), and the Ubl:S5a-UIM-2 complex. The HHR23A Ubl domain is structurally similar to ubiquitin. The S5a UIM forms an alpha-helix with an unexpected hairpin loop that contributes to the binding interface with Ubl. The molecular determinants of the Ubl-proteasome interaction are revealed by analysis of the structures, chemical shift mapping, mutant binding studies and sequence conservation. PubMed: 12970176DOI: 10.1093/emboj/cdg467 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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