Solution structure of the ubiquitin‐like domain of human DC‐UbP from dendritic cells

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.

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