Back to Search Start Over

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

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

Authors :
Gao, Yong-Guang
Song, Ai-Xin
Shi, Yan-Hong
Chang, Yong-Gang
Liu, Shu-Xun
Yu, Yi-Zi
Cao, Xue-Tao
Lin, Dong-Hai
Hu, Hong-Yu
Source :
Protein Science: A Publication of the Protein Society; 2005, Vol. 14 Issue 8, p2044-2050, 7p
Publication Year :
2005

Abstract

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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
09618368
Volume :
14
Issue :
8
Database :
Complementary Index
Journal :
Protein Science: A Publication of the Protein Society
Publication Type :
Academic Journal
Accession number :
90754812
Full Text :
https://doi.org/10.1110/ps.051455505