Structural origin for the transcriptional activity of human p53

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dc.contributor.authorSi Hyung Lee-
dc.contributor.authorKyu Hwan Park-
dc.contributor.authorDo Hyung Kim-
dc.contributor.authorDong Ho Choung-
dc.contributor.authorJae Eun Suk-
dc.contributor.authorDo Hyung Kim-
dc.contributor.authorJun Chang-
dc.contributor.authorYoung Chul Sung-
dc.contributor.authorKwan Yong Choi-
dc.contributor.authorKyou Hoon Han-
dc.date.accessioned2017-04-19T08:57:52Z-
dc.date.available2017-04-19T08:57:52Z-
dc.date.issued2001-
dc.identifier.issn1225-8687-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/5421-
dc.description.abstractTranscriptional activation domains are known to be inherently "unstructured" with no tertiary structure. A recent NMR study, however, has shown that the transactivation domain in human p53 is populated with an amphipathic helix and two nascent turns. This suggests that the presence of such local secondary structures within the overall "unstructured" structural framework is a general feature of acidic transactivation domains. These pre-existing local structures in p53, formed selectively by positionally conserved hydrophobic residues that are known to be critical for transcriptional activity, thus appear to constitute the specific structural motifs that regulate recognition of the p53 transactivation domain by target proteins. Here, we report the results of a NMR structural comparison between the native human p53 transactivation domain and an inactive mutant (22L,23W→22R,23S). Results show that the mutant has an identical overall structural topology as the native protein, to the extent that the amphipathic helix formed by the residues 18T-26L within the native p53 transactivating domain is preserved in the double mutant. Therefore, the lack of transcriptional activity in the double mutant should be ascribed to the disruption of the essential hydrophobic contacts between the p53 transactivation domain and target proteins due to the (22L,23W→22R,23S) mutation.-
dc.publisherKorea Soc-Assoc-Inst-
dc.titleStructural origin for the transcriptional activity of human p53-
dc.title.alternativeStructural origin for the transcriptional activity of human p53-
dc.typeArticle-
dc.citation.titleBMB Reports-
dc.citation.number1-
dc.citation.endPage79-
dc.citation.startPage73-
dc.citation.volume34-
dc.contributor.affiliatedAuthorSi Hyung Lee-
dc.contributor.affiliatedAuthorKyu Hwan Park-
dc.contributor.affiliatedAuthorDo Hyung Kim-
dc.contributor.affiliatedAuthorDong Ho Choung-
dc.contributor.affiliatedAuthorJae Eun Suk-
dc.contributor.affiliatedAuthorKyou Hoon Han-
dc.contributor.alternativeName이시형-
dc.contributor.alternativeName박규환-
dc.contributor.alternativeName김도형-
dc.contributor.alternativeName정동호-
dc.contributor.alternativeName석재은-
dc.contributor.alternativeName김도형-
dc.contributor.alternativeName장준-
dc.contributor.alternativeName성영철-
dc.contributor.alternativeName최관영-
dc.contributor.alternativeName한규훈-
dc.identifier.bibliographicCitationBMB Reports, vol. 34, no. 1, pp. 73-79-
dc.subject.keywordmouse double minute 2-
dc.subject.keywordnuclear magnetic resonance-
dc.subject.keywordp53-
dc.subject.keywordtranscriptional activation domain-
dc.subject.keywordUnstructured-
dc.subject.localmouse double minute 2-
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.localP53-
dc.subject.localp53-
dc.subject.localTranscriptional activation domain-
dc.subject.localtranscriptional activation domain-
dc.subject.localUnstructured-
dc.description.journalClassY-
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Division of Bio Technology Innovation > Core Research Facility & Analysis Center > 1. Journal Articles
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