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Article: Backbone and side-chain 1H, 13C and 15N assignments of the ubiquitin-associated domain of human X-linked inhibitor of apoptosis protein

TitleBackbone and side-chain 1H, 13C and 15N assignments of the ubiquitin-associated domain of human X-linked inhibitor of apoptosis protein
Authors
KeywordsNMR spectroscopy
Resonance assignment
Ubiquitin-associated (UBA) domain
X-linked Inhibitor of Apoptosis Protein (XIAP)
Issue Date2010
PublisherSpringer Netherlands. The Journal's web site is located at http://www.springer.com/physics/biophysics/journal/12104
Citation
Biomolecular Nmr Assignments, 2010, v. 4 n. 1, p. 13-15 How to Cite?
AbstractX-linked inhibitor of apoptosis protein (XIAP), a leading member of the family of inhibitor of apoptosis (IAP) proteins, is considered as the most potent and versatile inhibitor of caspases and apoptosis. It has been reported that XIAP is frequently overexpressed in cancer and its expression level is implicated in contributing to tumorigenesis, disease progression, chemoresistance and poor patient-survival. Therefore, XIAP is one of the leading targets in drug development for cancer therapy. Recently, based on bioinformatics study, a previously unrecognized but evolutionarily conserved ubiquitin-associated (UBA) domain in IAPs was identified. The UBA domain is found to be essential for the oncogenic potential of IAP, to maintain endothelial cell survival and to protect cells from TNF-α-induced apoptosis. Moreover, the UBA domain is required for XIAP to activate NF-κB. In the present study, we report the near complete resonance assignments of the UBA domain-containing region of human XIAP protein. Secondary structure prediction based on chemical shift index (CSI) analysis reveals that the protein is predominately α-helical, which is consistent with the structures of known UBA proteins. © 2009 Springer Science+Business Media B.V.
Persistent Identifierhttp://hdl.handle.net/10722/124007
ISSN
2015 Impact Factor: 0.687
2015 SCImago Journal Rankings: 0.325
PubMed Central ID
ISI Accession Number ID
Funding AgencyGrant Number
Hong Kong University
Research Grants Council of Hong KongHKU 7533/06 M
HKU 7755/08 M
Funding Information:

This work was supported by grants from the Hong Kong University Research Grant (KH Sze) and the Research Grants Council of Hong Kong for KH Sze (HKU 7533/06 M, HKU 7755/08 M).

References

 

DC FieldValueLanguage
dc.contributor.authorHui, SKen_HK
dc.contributor.authorTse, MKen_HK
dc.contributor.authorYang, Yen_HK
dc.contributor.authorWong, BCYen_HK
dc.contributor.authorSze, KHen_HK
dc.date.accessioned2010-10-19T04:32:37Z-
dc.date.available2010-10-19T04:32:37Z-
dc.date.issued2010en_HK
dc.identifier.citationBiomolecular Nmr Assignments, 2010, v. 4 n. 1, p. 13-15en_HK
dc.identifier.issn1874-2718en_HK
dc.identifier.urihttp://hdl.handle.net/10722/124007-
dc.description.abstractX-linked inhibitor of apoptosis protein (XIAP), a leading member of the family of inhibitor of apoptosis (IAP) proteins, is considered as the most potent and versatile inhibitor of caspases and apoptosis. It has been reported that XIAP is frequently overexpressed in cancer and its expression level is implicated in contributing to tumorigenesis, disease progression, chemoresistance and poor patient-survival. Therefore, XIAP is one of the leading targets in drug development for cancer therapy. Recently, based on bioinformatics study, a previously unrecognized but evolutionarily conserved ubiquitin-associated (UBA) domain in IAPs was identified. The UBA domain is found to be essential for the oncogenic potential of IAP, to maintain endothelial cell survival and to protect cells from TNF-α-induced apoptosis. Moreover, the UBA domain is required for XIAP to activate NF-κB. In the present study, we report the near complete resonance assignments of the UBA domain-containing region of human XIAP protein. Secondary structure prediction based on chemical shift index (CSI) analysis reveals that the protein is predominately α-helical, which is consistent with the structures of known UBA proteins. © 2009 Springer Science+Business Media B.V.en_HK
dc.languageengen_HK
dc.publisherSpringer Netherlands. The Journal's web site is located at http://www.springer.com/physics/biophysics/journal/12104en_HK
dc.relation.ispartofBiomolecular NMR Assignmentsen_HK
dc.rightsSpringer Science+Business Media B.V.en_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subjectNMR spectroscopyen_HK
dc.subjectResonance assignmenten_HK
dc.subjectUbiquitin-associated (UBA) domainen_HK
dc.subjectX-linked Inhibitor of Apoptosis Protein (XIAP)en_HK
dc.titleBackbone and side-chain 1H, 13C and 15N assignments of the ubiquitin-associated domain of human X-linked inhibitor of apoptosis proteinen_HK
dc.typeArticleen_HK
dc.identifier.emailWong, BCY:bcywong@hku.hken_HK
dc.identifier.emailSze, KH:khsze@hku.hken_HK
dc.identifier.authorityWong, BCY=rp00429en_HK
dc.identifier.authoritySze, KH=rp00785en_HK
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1007/s12104-009-9197-xen_HK
dc.identifier.pmid19916060-
dc.identifier.pmcidPMC2946540-
dc.identifier.scopuseid_2-s2.0-77951879746en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-77951879746&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume4en_HK
dc.identifier.issue1en_HK
dc.identifier.spage13en_HK
dc.identifier.epage15en_HK
dc.identifier.eissn1874-270Xen_HK
dc.identifier.isiWOS:000277227800004-
dc.publisher.placeNetherlandsen_HK
dc.description.otherSpringer Open Choice, 01 Dec 2010-
dc.identifier.scopusauthoridHui, SK=13406279000en_HK
dc.identifier.scopusauthoridTse, MK=36437795000en_HK
dc.identifier.scopusauthoridYang, Y=7409391816en_HK
dc.identifier.scopusauthoridWong, BCY=7402023340en_HK
dc.identifier.scopusauthoridSze, KH=7006735061en_HK
dc.identifier.citeulike6186675-

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