1TTN
Solution structure of the ubiquitin-like domain of human DC-UBP from dendritic cells
Summary for 1TTN
| Entry DOI | 10.2210/pdb1ttn/pdb |
| NMR Information | BMRB: 6609 |
| Descriptor | dendritic cell-derived ubiquitin-like protein (1 entity in total) |
| Functional Keywords | ubiquitin-like domain, dc-ubp, solution structure, signaling protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: Q8WUN7 |
| Total number of polymer chains | 1 |
| Total formula weight | 12180.95 |
| Authors | Hu, H.Y. (deposition date: 2004-06-23, release date: 2005-07-05, Last modification date: 2024-05-29) |
| Primary citation | Gao, Y.G.,Song, A.X.,Shi, Y.H.,Chang, Y.G.,Liu, S.X.,Yu, Y.Z.,Cao, X.T.,Lin, D.H.,Hu, H.Y. Solution structure of the ubiquitin-like domain of human DC-UbP from dendritic cells Protein Sci., 14:2044-2050, 2005 Cited by PubMed Abstract: The previously identified dendritic cell-derived ubiquitin-like protein (DC-UbP) was implicated in cellular differentiation and apoptosis. Sequence alignment suggested that it contains a ubiquitin-like (UbL) domain in the C terminus. Here, we present the solution NMR structure and backbone dynamics of the UbL domain of DC-UbP. The overall structure of the domain is very similar to that of Ub despite low similarity (<30%) in amino-acid sequence. One distinct feature of the domain structure is its highly positively charged surface that is different from the corresponding surfaces of the well-known UbL modifiers, Ub, NEDD8, and SUMO-1. The key amino-acid residues responsible for guiding polyubiquitinated proteins to proteasome degradation in Ub are not conserved in the UbL domain. This implies that the UbL domain of DC-UbP may have its own specific interaction partners with other yet unknown cellular functions related to the Ub pathway. PubMed: 15987890DOI: 10.1110/ps.051455505 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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