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.
Original language | English (US) |
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Pages (from-to) | 2044-2050 |
Number of pages | 7 |
Journal | Protein Science |
Volume | 14 |
Issue number | 8 |
DOIs | |
State | Published - Aug 2005 |
Keywords
- DC-Ubp
- Dynamics
- NMR
- Solution structure
- Ubiquitin-like domain