Structural investigation on the intrinsically disordered N-terminal region of HPV16 E7 protein

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dc.contributor.authorChewook Lee-
dc.contributor.authorDo-Hyoung Kim-
dc.contributor.authorSi-Hyung Lee-
dc.contributor.authorJ Su-
dc.contributor.authorKyou Hoon Han-
dc.date.accessioned2017-04-19T10:30:15Z-
dc.date.available2017-04-19T10:30:15Z-
dc.date.issued2016-
dc.identifier.issn1225-8687-
dc.identifier.uri10.5483/BMBRep.2016.49.8.021ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/13554-
dc.description.abstractHuman papillomavirus (HPV) is the major cause of cervical cancer, a deadly threat to millions of females. The early oncogene product (E7) of the high-risk HPV16 is the primary agent associated with HPV-related cervical cancers. In order to understand how E7 contributes to the transforming activity, we investigated the structural features of the flexible N-terminal region (46 residues) of E7 by carrying out N-15 heteronuclear NMR experiments and replica exchange molecular dynamics simulations. Several NMR parameters as well as simulation ensemble structures indicate that this intrinsically disordered region of E7 contains two transient (10-20% populated) helical pre-structured motifs that overlap with important target binding moieties such as an E2F-mimic motif and a pRb-binding LXCXE segment. Presence of such target-binding motifs in HPV16 E7 provides a reasonable explanation for its promiscuous target-binding behavior associated with its transforming activity.-
dc.publisherKorea Soc-Assoc-Inst-
dc.titleStructural investigation on the intrinsically disordered N-terminal region of HPV16 E7 protein-
dc.title.alternativeStructural investigation on the intrinsically disordered N-terminal region of HPV16 E7 protein-
dc.typeArticle-
dc.citation.titleBMB Reports-
dc.citation.number8-
dc.citation.endPage436-
dc.citation.startPage431-
dc.citation.volume49-
dc.contributor.affiliatedAuthorChewook Lee-
dc.contributor.affiliatedAuthorDo-Hyoung Kim-
dc.contributor.affiliatedAuthorSi-Hyung Lee-
dc.contributor.affiliatedAuthorKyou Hoon Han-
dc.contributor.alternativeName이제욱-
dc.contributor.alternativeName김도형-
dc.contributor.alternativeName이시형-
dc.contributor.alternativeNameSu-
dc.contributor.alternativeName한규훈-
dc.identifier.bibliographicCitationBMB Reports, vol. 49, no. 8, pp. 431-436-
dc.identifier.doi10.5483/BMBRep.2016.49.8.021-
dc.subject.keywordE7 oncoprotein-
dc.subject.keywordHuman papillomavirus (HPV)-
dc.subject.keywordIntrinsically disordered protein (IDP)-
dc.subject.keywordMolecular dynamics (MD) simulation-
dc.subject.keywordNuclear magnetic resonance (NMR)-
dc.subject.keywordPre-structured motif (PreSMo)-
dc.subject.localE7 oncoprotein-
dc.subject.localhuman papillomavirus (HPV)-
dc.subject.localHuman papillomavirus-
dc.subject.localhuman paillomavirus(HPV)-
dc.subject.localhuman papillomavirus-
dc.subject.localHuman papillomavirus (HPV)-
dc.subject.localhuman papilloma virus (HPV)-
dc.subject.localHPV-
dc.subject.localintrinsically disordered protein-
dc.subject.localIntrinsically disordered protein (IDP)-
dc.subject.localIntrinsically disordered protein-
dc.subject.localintrinsically disordered protein (IDP)-
dc.subject.localMolecular dynamics (MD) simulation-
dc.subject.localMolecular dynamics simulation-
dc.subject.localMolecular dynamics simulations-
dc.subject.localMolecular Dynamics (MD) simulations-
dc.subject.localNMR-
dc.subject.localnuclear magnetic resonance (Nmr)-
dc.subject.localNuclear magnetic resonance-
dc.subject.localnuclear magnetic resonance-
dc.subject.localNuclear magnetic resonance (NMR)-
dc.subject.localPreSMos (Pre-Structured Motifs)-
dc.subject.localPre-structured motif-
dc.subject.localPrestructured motif (PreSMo)-
dc.subject.localPre-structured motif (PreSMo)-
dc.subject.localPreSMo (Pre-Structured Motif)-
dc.subject.localpre-structured motif-
dc.subject.localpre-structured motifs (PreSMos)-
dc.subject.localPre-Structured Motif (PreSMo)-
dc.subject.localPreSMo-
dc.subject.localPreSMos (pre-structured motifs)-
dc.description.journalClassY-
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Division of Bio Technology Innovation > Core Research Facility & Analysis Center > 1. Journal Articles
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