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


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.

SUBMITTER: Gao YG 

PROVIDER: S-EPMC2279315 | biostudies-literature | 2005 Aug

REPOSITORIES: biostudies-literature

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

Gao Yong-Guang YG   Song Ai-Xin AX   Shi Yan-Hong YH   Chang Yong-Gang YG   Liu Shu-Xun SX   Yu Yi-Zi YZ   Cao Xue-Tao XT   Lin Dong-Hai DH   Hu Hong-Yu HY  

Protein science : a publication of the Protein Society 20050629 8


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  ...[more]

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