Solution structure of the ubiquitin-like domain of human DC-UbP from dendritic cells |
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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 |
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Affiliation: | Key Laboratory of Proteomics, Institute of Biochemsitry and Cell Biology, Shanghai Institutes for Biological Sciences, Shanghai 200031, People's Republic of China. |
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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. |
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Keywords: | solution structure dynamics ubiquitin-like domain DC-UbP NMR |
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