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- Publisher Website: 10.1002/pro.386
- Scopus: eid_2-s2.0-79958140557
- PMID: 20440844
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Article: Solution structure of the N-terminal domain of DC-UbP/UBTD2 and its interaction with ubiquitin
Title | Solution structure of the N-terminal domain of DC-UbP/UBTD2 and its interaction with ubiquitin |
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Authors | |
Issue Date | 2010 |
Publisher | Wiley-Blackwell Publishing, Inc.. The Journal's web site is located at http://www.proteinscience.org |
Citation | Protein Science, 2010, v. 19 n. 5, p. 1104-1109 How to Cite? |
Abstract | 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. |
Persistent Identifier | http://hdl.handle.net/10722/197581 |
ISSN | 2023 Impact Factor: 4.5 2023 SCImago Journal Rankings: 4.419 |
PubMed Central ID | |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Song, AX | - |
dc.contributor.author | Zhou, CJ | - |
dc.contributor.author | Guan, X | - |
dc.contributor.author | Sze, KH | - |
dc.contributor.author | Hu, HY | - |
dc.date.accessioned | 2014-05-29T08:14:06Z | - |
dc.date.available | 2014-05-29T08:14:06Z | - |
dc.date.issued | 2010 | - |
dc.identifier.citation | Protein Science, 2010, v. 19 n. 5, p. 1104-1109 | - |
dc.identifier.issn | 0961-8368 | - |
dc.identifier.uri | http://hdl.handle.net/10722/197581 | - |
dc.description.abstract | 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. | - |
dc.language | eng | - |
dc.publisher | Wiley-Blackwell Publishing, Inc.. The Journal's web site is located at http://www.proteinscience.org | - |
dc.relation.ispartof | Protein Science | - |
dc.rights | The definitive version is available at www3.interscience.wiley.com | - |
dc.subject.mesh | Dendritic Cells - chemistry | - |
dc.subject.mesh | Nuclear Magnetic Resonance, Biomolecular - methods | - |
dc.subject.mesh | Protein Structure, Tertiary - genetics | - |
dc.subject.mesh | Ubiquitin - chemistry - metabolism | - |
dc.subject.mesh | Ubiquitins - chemistry - genetics - metabolism | - |
dc.title | Solution structure of the N-terminal domain of DC-UbP/UBTD2 and its interaction with ubiquitin | en_US |
dc.type | Article | en_US |
dc.identifier.email | Sze, KH: khsze@hku.hk | - |
dc.identifier.email | Hu, HY: hyhu@sibs.ac.cn | - |
dc.description.nature | link_to_OA_fulltext | - |
dc.identifier.doi | 10.1002/pro.386 | - |
dc.identifier.pmid | 20440844 | - |
dc.identifier.pmcid | PMC2868252 | - |
dc.identifier.scopus | eid_2-s2.0-79958140557 | - |
dc.identifier.hkuros | 172734 | - |
dc.identifier.volume | 19 | - |
dc.identifier.issue | 5 | - |
dc.identifier.spage | 1104 | - |
dc.identifier.epage | 1109 | - |
dc.identifier.isi | WOS:000277279500019 | - |
dc.publisher.place | United States | - |
dc.identifier.issnl | 0961-8368 | - |