Solution structure of the N-terminal domain of DC-UbP/UBTD2 and its interaction with ubiquitin.
DC-UbP/UBTD2 is a ubiquitin (Ub) domain-containing protein first identified from dendritic cells, and is implicated in ubiquitination pathway. The solution structure and backbone dynamics of the C-terminal Ub-like (UbL) domain were elucidated in our previous work. To further understand the biological function of DC-UbP, we then solved the solution structure ... of the N-terminal domain of DC-UbP (DC-UbP_N) and studied its Ub binding properties by NMR techniques. The results show that DC-UbP_N holds a novel structural fold and acts as a Ub-binding domain (UBD) but with low affinity. This implies that the DC-UbP protein, composing of a combination of both UbL and UBD domains, might play an important role in regulating protein ubiquitination and delivery of ubiquitinated substrates in eukaryotic cells.
Mesh Terms:
Dendritic Cells, Escherichia coli, Humans, Models, Molecular, Models, Statistical, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Tertiary, Recombinant Proteins, Ubiquitin, Ubiquitins
Dendritic Cells, Escherichia coli, Humans, Models, Molecular, Models, Statistical, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Tertiary, Recombinant Proteins, Ubiquitin, Ubiquitins
Protein Sci.
Date: May. 01, 2010
PubMed ID: 20440844
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