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 journalArticleResearchpeer-review

6 Citations (Scopus)


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
Pages (from-to)2044-2050
Number of pages7
JournalProtein Science
Issue number8
Publication statusPublished - Aug 2005
Externally publishedYes


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

Cite this