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1TTN

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

Summary for 1TTN
Entry DOI10.2210/pdb1ttn/pdb
NMR InformationBMRB: 6609
Descriptordendritic cell-derived ubiquitin-like protein (1 entity in total)
Functional Keywordsubiquitin-like domain, dc-ubp, solution structure, signaling protein
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm: Q8WUN7
Total number of polymer chains1
Total formula weight12180.95
Authors
Hu, H.Y. (deposition date: 2004-06-23, release date: 2005-07-05, Last modification date: 2024-05-29)
Primary citationGao, Y.G.,Song, A.X.,Shi, Y.H.,Chang, Y.G.,Liu, S.X.,Yu, Y.Z.,Cao, X.T.,Lin, D.H.,Hu, H.Y.
Solution structure of the ubiquitin-like domain of human DC-UbP from dendritic cells
Protein Sci., 14:2044-2050, 2005
Cited by
PubMed 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.
PubMed: 15987890
DOI: 10.1110/ps.051455505
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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