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.
Key Laboratory of Proteomics, Institute of Biochemsitry and Cell Biology, Shanghai Institutes for Biological Sciences, Shanghai 200031, People's Republic of China.
Yong-Guang
YG
Gao
Ai-Xin
AX
Song
Yan-Hong
YH
Shi
Yong-Gang
YG
Chang
Shu-Xun
SX
Liu
Yi-Zi
YZ
Yu
Xue-Tao
XT
Cao
Dong-Hai
DH
Lin
Hong-Yu
HY
Hu
D000595:Amino Acid Sequence; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D012996:Solutions; D055672:Static Electricity; D025801:Ubiquitin / Q000737:chemistry; D014452:Ubiquitins / Q000737:chemistry*
D009419:Nerve Tissue Proteins; D012996:Solutions; C471042:UBTD2 protein, human; D025801:Ubiquitin; D014452:Ubiquitins