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Article: Structure of human upstream binding factor HMG box 5 and site for binding of the cell-cycle regulatory factor TAF1

TitleStructure of human upstream binding factor HMG box 5 and site for binding of the cell-cycle regulatory factor TAF1
Authors
KeywordsCell-cycle regulation
High-mobility group protein
Human upstream binding factor
Protein-protein interactions
RNA polymerases
Single-wavelength anomalous dispersion
TATA-binding protein
TBP-assiociated factor 1
Issue Date2007
PublisherWiley-Blackwell Publishing, Inc.. The Journal's web site is located at http://www.wiley.com/bw/editors.asp?ref=0907-4449&site=1
Citation
Acta Crystallographica Section D: Biological Crystallography, 2007, v. 63 n. 6, p. 730-737 How to Cite?
AbstractThe fifth HMG-box domain in human upstream binding factor (hUBF) contributes to the synthesis of rRNA by RNA polymerase I (Pol I). The 2.0 Å resolution crystal structure of this protein has been solved using the single-wavelength anomalous dispersion method (SAD). The crystal structure and the reported NMR structure have r.m.s. deviations of 2.18-3.03 Å for the C α atoms. However, there are significant differences between the two structures, with displacements of up to 9.0 Å. Compared with other HMG-box structures, the r.m.s. deviations for C α atoms between hUBF HMG box 5 and HMG domains from Drosophila melanogaster protein D and Rattus norvegicus HMG1 are 1.5 and 1.6 Å, respectively. This indicates that the differences between the crystal and NMR structures of hUBF HMG box 5 are larger than those with its homologous structures. The differences between the two structures potentially reflect two states with different structures. The specific interactions between the hUBF HMG box 5 and the first bromodomain of TBP-associated factor 1 (TAF1) were studied by ultrasensitive differential scanning calorimetry and chemical shift perturbation. Based on these experimental data, possible sites in hUBF HMG box 5 that may interact with the first bromodomain of TAF1 were proposed. © International Union of Crystallography 2007.
Persistent Identifierhttp://hdl.handle.net/10722/91892
ISSN
2013 Impact Factor: 7.232
2015 SCImago Journal Rankings: 3.088
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorRong, Hen_HK
dc.contributor.authorLi, Yen_HK
dc.contributor.authorShi, Xen_HK
dc.contributor.authorZhang, Xen_HK
dc.contributor.authorGao, Yen_HK
dc.contributor.authorDai, Hen_HK
dc.contributor.authorTeng, Men_HK
dc.contributor.authorNiu, Len_HK
dc.contributor.authorLiu, Qen_HK
dc.contributor.authorHao, Qen_HK
dc.date.accessioned2010-09-17T10:29:43Z-
dc.date.available2010-09-17T10:29:43Z-
dc.date.issued2007en_HK
dc.identifier.citationActa Crystallographica Section D: Biological Crystallography, 2007, v. 63 n. 6, p. 730-737en_HK
dc.identifier.issn0907-4449en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91892-
dc.description.abstractThe fifth HMG-box domain in human upstream binding factor (hUBF) contributes to the synthesis of rRNA by RNA polymerase I (Pol I). The 2.0 Å resolution crystal structure of this protein has been solved using the single-wavelength anomalous dispersion method (SAD). The crystal structure and the reported NMR structure have r.m.s. deviations of 2.18-3.03 Å for the C α atoms. However, there are significant differences between the two structures, with displacements of up to 9.0 Å. Compared with other HMG-box structures, the r.m.s. deviations for C α atoms between hUBF HMG box 5 and HMG domains from Drosophila melanogaster protein D and Rattus norvegicus HMG1 are 1.5 and 1.6 Å, respectively. This indicates that the differences between the crystal and NMR structures of hUBF HMG box 5 are larger than those with its homologous structures. The differences between the two structures potentially reflect two states with different structures. The specific interactions between the hUBF HMG box 5 and the first bromodomain of TBP-associated factor 1 (TAF1) were studied by ultrasensitive differential scanning calorimetry and chemical shift perturbation. Based on these experimental data, possible sites in hUBF HMG box 5 that may interact with the first bromodomain of TAF1 were proposed. © International Union of Crystallography 2007.en_HK
dc.languageengen_HK
dc.publisherWiley-Blackwell Publishing, Inc.. The Journal's web site is located at http://www.wiley.com/bw/editors.asp?ref=0907-4449&site=1en_HK
dc.relation.ispartofActa Crystallographica Section D: Biological Crystallographyen_HK
dc.subjectCell-cycle regulationen_HK
dc.subjectHigh-mobility group proteinen_HK
dc.subjectHuman upstream binding factoren_HK
dc.subjectProtein-protein interactionsen_HK
dc.subjectRNA polymerasesen_HK
dc.subjectSingle-wavelength anomalous dispersionen_HK
dc.subjectTATA-binding proteinen_HK
dc.subjectTBP-assiociated factor 1en_HK
dc.titleStructure of human upstream binding factor HMG box 5 and site for binding of the cell-cycle regulatory factor TAF1en_HK
dc.typeArticleen_HK
dc.identifier.emailHao, Q: qhao@hku.hken_HK
dc.identifier.authorityHao, Q=rp01332en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1107/S0907444907017027en_HK
dc.identifier.pmid17505112-
dc.identifier.scopuseid_2-s2.0-34249020675en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-34249020675&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume63en_HK
dc.identifier.issue6en_HK
dc.identifier.spage730en_HK
dc.identifier.epage737en_HK
dc.identifier.isiWOS:000248009200009-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridRong, H=12799414200en_HK
dc.identifier.scopusauthoridLi, Y=24776012100en_HK
dc.identifier.scopusauthoridShi, X=54912481900en_HK
dc.identifier.scopusauthoridZhang, X=36071931400en_HK
dc.identifier.scopusauthoridGao, Y=35731144800en_HK
dc.identifier.scopusauthoridDai, H=8279963100en_HK
dc.identifier.scopusauthoridTeng, M=7101891754en_HK
dc.identifier.scopusauthoridNiu, L=7101760477en_HK
dc.identifier.scopusauthoridLiu, Q=35215401600en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK
dc.identifier.citeulike1256178-

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