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

Yong Guang Gao, A. I Xin Song, Yan Hong Shi, Yong Gang Chang, Shu Xun Liu, Y. I Z I Yu, Xue Tao Cao, Dong Hai Lin, Hong Yu Hu

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


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 languageEnglish (US)
Pages (from-to)2044-2050
Number of pages7
JournalProtein Science
Issue number8
StatePublished - Aug 2005


  • DC-Ubp
  • Dynamics
  • NMR
  • Solution structure
  • Ubiquitin-like domain


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