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dc.contributor.CRUESPUniversidade Estadual de Campinaspt_BR
dc.typeArtigo de periódicopt_BR
dc.titleExpression and spectroscopic analysis of a mutant hepatitis B virus onco-protein HBx without cysteine residuespt_BR
dc.contributor.authorRui, Ept_BR
dc.contributor.authorde Moura, PRpt_BR
dc.contributor.authorGoncalves, KDpt_BR
dc.contributor.authorKobarg, Jpt_BR
unicamp.author.emailjkobarg@lnls.brpt_BR
unicamp.authorLab Nacl Luz Sincrotron, Ctr Biol Mol Estrutural, BR-13084971 Campinas, SP, Brazil Univ Estadual Campinas, Inst Biol, Dept Bioquim, Campinas, SP, Brazilpt_BR
dc.subjectviral hepatitispt_BR
dc.subjecthepatitis B virus X proteinpt_BR
dc.subjectviral transactivatorpt_BR
dc.subjectonco-proteinpt_BR
dc.subjectcircular dichroismpt_BR
dc.subjectfluorescencept_BR
dc.subject.wosTata-binding Proteinpt_BR
dc.subject.wosLong Terminal Repeatpt_BR
dc.subject.wosRetinoid-x-receptorpt_BR
dc.subject.wosHepatocellular-carcinomapt_BR
dc.subject.wosDna-bindingpt_BR
dc.subject.wosEscherichia-colipt_BR
dc.subject.wosTransactivator Proteinpt_BR
dc.subject.wosViral-infectionpt_BR
dc.subject.wosDamaged Dnapt_BR
dc.subject.wosLiver-cellspt_BR
dc.description.abstractChronic infection of the hepatitis B virus (HBV) is one of the causes leading to liver cancer. The 3.2 kb genome of HBV encodes four proteins: core antigen, surface antigen, a DNA polymerase and the X protein (HBx). The biological functions of HBx are not fully understood. It has been shown that HBx is a potent trans -activator, which activates transcription of many cellular and viral promoters indirectly via protein-protein interactions. These transactivating activities of HBx may contribute to the development of hepatocellular carcinoma. In this paper a truncated mini-HBx(-Cys) ( 18-142) protein, where the cysteines had been either deleted or substituted by serines, was constructed by site-directed mutagenesis and overexpressed as a 6xHis fusion protein in Escherichia coli. The 6xHis-mini-HBx(-Cys) protein was isolated from inclusion bodies, purified by Ni-affinity chromatography under denaturing conditions and refolded by sequential dialysis. The structure of the 6xHis-mini-HBx(-Cys) protein was analyzed by circular dichroism, fluorescence and one-dimensional NMR spectroscopic assays. The data presented here suggest that HBx is unstructured but has a propensity to gain secondary structure under specific experimental conditions. Its conformational flexibility might partially explain its functional complexity, namely its capacity to interact with a wide array of signaling proteins, transcriptional regulators and nucleic acids. © 2005 Elsevier B.V. All rights reserved.pt
dc.relation.ispartofJournal Of Virological Methodspt_BR
dc.relation.ispartofabbreviationJ. Virol. Methodspt_BR
dc.publisher.cityAmsterdampt_BR
dc.publisher.countryHolandapt_BR
dc.publisherElsevier Science Bvpt_BR
dc.date.issued2005pt_BR
dc.date.monthofcirculationJUNpt_BR
dc.identifier.citationJournal Of Virological Methods. Elsevier Science Bv, v. 126, n. 41671, n. 65, n. 74, 2005.pt_BR
dc.language.isoenpt_BR
dc.description.volume126pt_BR
dc.description.issuenumber41671pt_BR
dc.description.firstpage65pt_BR
dc.description.lastpage74pt_BR
dc.rightsfechadopt_BR
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policypt_BR
dc.sourceWeb of Sciencept_BR
dc.identifier.issn0166-0934pt_BR
dc.identifier.wosidWOS:000229003000008pt_BR
dc.identifier.doi10.1016/j.jviromet.2005.01.022pt_BR
dc.date.available2014-11-18T03:05:16Z
dc.date.available2015-11-26T17:45:38Z-
dc.date.accessioned2014-11-18T03:05:16Z
dc.date.accessioned2015-11-26T17:45:38Z-
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dc.description.provenanceMade available in DSpace on 2015-11-26T17:45:38Z (GMT). No. of bitstreams: 2 WOS000229003000008.pdf: 384281 bytes, checksum: 46ef621f62762a379cb69ad12b4031df (MD5) WOS000229003000008.pdf.txt: 49799 bytes, checksum: 3f982bffed6030889836e5b9ad5391cd (MD5) Previous issue date: 2005en
dc.identifier.urihttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/66456pt_BR
dc.identifier.urihttp://www.repositorio.unicamp.br/handle/REPOSIP/66456
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/66456-
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