The MDM2-binding region in the transactivation domain of p53 also acts as a Bcl-X-L-binding motif

Cited 32 time in scopus
Metadata Downloads

Full metadata record

DC FieldValueLanguage
dc.contributor.authorH Xu-
dc.contributor.authorH Ye-
dc.contributor.authorN E Osman-
dc.contributor.authorK Sadler-
dc.contributor.authorEunyoung Won-
dc.contributor.authorSeung-Wook Chi-
dc.contributor.authorH S Yoon-
dc.date.accessioned2017-04-19T09:17:07Z-
dc.date.available2017-04-19T09:17:07Z-
dc.date.issued2009-
dc.identifier.issn0006-2960-
dc.identifier.uri10.1021/bi901188sko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/9329-
dc.description.abstractWhile the transcription-dependent mechanism of p53 has been extensively studied, recently the transcription-independent apoptotic activity of p53 has also been described. Bcl-2 and Bcl-XL interact with p53 and induce apoptosis. Initially, the p53 DNA-binding domain (p53DBD) was found to bind to Bcl-2 and Bcl-XL. Later, the p53 N-terminal domain (p53NTD) was reported to be sufficient for inducing the transcription-independent apoptotic activity of p53 and also shown to interact with Bcl-XL. Here, we further document that the transactivation domain of p53 (p53TAD) in p53NTD alone binds to Bcl-XL. We demonstrated that the MDM2-binding region (residues S15 to N29, herein referred to as SN15) in p53TAD is the binding site for Bcl-XL. The binding interface on Bcl-XL was identified at the hydrophobic pocket formed by the BH1, BH2, and BH3 domains, which also binds to the Bak/Bad BH3 peptides, suggesting Bcl-XL and MDM2 share a common binding motif in p53TAD. OurNMR structural studies have shown that the SN15 peptide undergoes a conformational change upon binding to Bcl-X L. A Bcl-XL/SN15 complex structural model suggests that the SN15 peptide adopts an extended α-helical structure to bind to the hydrophobic pocket on the Bcl-XL, which is similar to the mode of binding between BH3 peptides and Bcl-XL.-
dc.publisherAmer Chem Soc-
dc.titleThe MDM2-binding region in the transactivation domain of p53 also acts as a Bcl-X-L-binding motif-
dc.title.alternativeThe MDM2-binding region in the transactivation domain of p53 also acts as a Bcl-X-L-binding motif-
dc.typeArticle-
dc.citation.titleBiochemistry-
dc.citation.number51-
dc.citation.endPage12168-
dc.citation.startPage12159-
dc.citation.volume48-
dc.contributor.affiliatedAuthorEunyoung Won-
dc.contributor.affiliatedAuthorSeung-Wook Chi-
dc.contributor.alternativeNameXu-
dc.contributor.alternativeNameYe-
dc.contributor.alternativeNameOsman-
dc.contributor.alternativeNameSadler-
dc.contributor.alternativeName원은영-
dc.contributor.alternativeName지승욱-
dc.contributor.alternativeName윤호섭-
dc.identifier.bibliographicCitationBiochemistry, vol. 48, no. 51, pp. 12159-12168-
dc.identifier.doi10.1021/bi901188s-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.