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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.
- 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