1ttn
From Proteopedia
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Solution structure of the ubiquitin-like domain of human DC-UBP from dendritic cells
Overview
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.
About this Structure
1TTN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of the ubiquitin-like domain of human DC-UbP from dendritic cells., Gao YG, Song AX, Shi YH, Chang YG, Liu SX, Yu YZ, Cao XT, Lin DH, Hu HY, Protein Sci. 2005 Aug;14(8):2044-50. Epub 2005 Jun 29. PMID:15987890
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