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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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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.[1]

References

  1. Solution structure of the ubiquitin-like domain of human DC-UbP from dendritic cells. 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. Protein Sci. (2005) [Pubmed]
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