Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Solution structure of the N-terminal domain of DC-UbP/UBTD2 and its interaction with ubiquitin.,Song AX, Zhou CJ, Guan X, Sze KH, Hu HY Protein Sci. 2010 May;19(5):1104-9. PMID:20440844[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Song AX, Zhou CJ, Guan X, Sze KH, Hu HY. Solution structure of the N-terminal domain of DC-UbP/UBTD2 and its interaction with ubiquitin. Protein Sci. 2010 May;19(5):1104-9. PMID:20440844 doi:10.1002/pro.386
