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Article: Solution structure of the N-terminal domain of DC-UbP/UBTD2 and its interaction with ubiquitin

TitleSolution structure of the N-terminal domain of DC-UbP/UBTD2 and its interaction with ubiquitin
Authors
Issue Date2010
PublisherWiley-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?
AbstractDC-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 Identifierhttp://hdl.handle.net/10722/197581
ISSN
2015 Impact Factor: 3.039
2015 SCImago Journal Rankings: 2.029
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorSong, AX-
dc.contributor.authorZhou, CJ-
dc.contributor.authorGuan, X-
dc.contributor.authorSze, KH-
dc.contributor.authorHu, HY-
dc.date.accessioned2014-05-29T08:14:06Z-
dc.date.available2014-05-29T08:14:06Z-
dc.date.issued2010-
dc.identifier.citationProtein Science, 2010, v. 19 n. 5, p. 1104-1109-
dc.identifier.issn0961-8368-
dc.identifier.urihttp://hdl.handle.net/10722/197581-
dc.description.abstractDC-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.languageeng-
dc.publisherWiley-Blackwell Publishing, Inc.. The Journal's web site is located at http://www.proteinscience.org-
dc.relation.ispartofProtein Science-
dc.rightsThe definitive version is available at www3.interscience.wiley.com-
dc.subject.meshDendritic Cells - chemistry-
dc.subject.meshNuclear Magnetic Resonance, Biomolecular - methods-
dc.subject.meshProtein Structure, Tertiary - genetics-
dc.subject.meshUbiquitin - chemistry - metabolism-
dc.subject.meshUbiquitins - chemistry - genetics - metabolism-
dc.titleSolution structure of the N-terminal domain of DC-UbP/UBTD2 and its interaction with ubiquitinen_US
dc.typeArticleen_US
dc.identifier.emailSze, KH: khsze@hku.hk-
dc.identifier.emailHu, HY: hyhu@sibs.ac.cn-
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1002/pro.386-
dc.identifier.pmid20440844-
dc.identifier.pmcidPMC2868252-
dc.identifier.scopuseid_2-s2.0-79958140557-
dc.identifier.hkuros172734-
dc.identifier.volume19-
dc.identifier.issue5-
dc.identifier.spage1104-
dc.identifier.epage1109-
dc.identifier.isiWOS:000277279500019-
dc.publisher.placeUnited States-

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