1IFY
Solution Structure of the Internal UBA Domain of HHR23A
Summary for 1IFY
| Entry DOI | 10.2210/pdb1ify/pdb |
| Related | 1DV0 1F4I |
| Descriptor | UV EXCISION REPAIR PROTEIN RAD23 HOMOLOG A (1 entity in total) |
| Functional Keywords | ubiquitin associated domain, uba domain, ubiquitin proteosome pathway, dna binding protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: P54725 |
| Total number of polymer chains | 1 |
| Total formula weight | 5496.23 |
| Authors | Mueller, T.D.,Feigon, J. (deposition date: 2001-04-13, release date: 2002-07-03, Last modification date: 2024-05-22) |
| Primary citation | Mueller, T.D.,Feigon, J. Solution structures of UBA domains reveal a conserved hydrophobic surface for protein-protein interactions. J.Mol.Biol., 319:1243-1255, 2002 Cited by PubMed Abstract: UBA domains are a commonly occurring sequence motif of approximately 45 amino acid residues that are found in diverse proteins involved in the ubiquitin/proteasome pathway, DNA excision-repair, and cell signaling via protein kinases. The human homologue of yeast Rad23A (HHR23A) is one example of a nucleotide excision-repair protein that contains both an internal and a C-terminal UBA domain. The solution structure of HHR23A UBA(2) showed that the domain forms a compact three-helix bundle. We report the structure of the internal UBA(1) domain of HHR23A. Comparison of the structures of UBA(1) and UBA(2) reveals that both form very similar folds and have a conserved large hydrophobic surface patch. The structural similarity between UBA(1) and UBA(2), in spite of their low level of sequence conservation, leads us to conclude that the structural variability of UBA domains in general is likely to be rather small. On the basis of the structural similarities as well as analysis of sequence conservation, we predict that this hydrophobic surface patch is a common protein-interacting surface present in diverse UBA domains. Furthermore, accumulating evidence that ubiquitin binds to UBA domains leads us to the prediction that the hydrophobic surface patch of UBA domains interacts with the hydrophobic surface on the five-stranded beta-sheet of ubiquitin. Detailed comparison of the structures of the two UBA domains, combined with previous mutagenesis studies, indicates that the binding site of HIV-1 Vpr on UBA(2) does not completely overlap the ubiquitin binding site. PubMed: 12079361DOI: 10.1016/S0022-2836(02)00302-9 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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