Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/87108
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dc.contributor.authorLee, Dong-Hwaen
dc.contributor.authorHa, Ji-Hyangen
dc.contributor.authorKim, Yulen
dc.contributor.authorJang, Mien
dc.contributor.authorPark, Sung Jeanen
dc.contributor.authorYoon, Ho Supen
dc.contributor.authorKim, Eun-Heeen
dc.contributor.authorBae, Kwang-Heeen
dc.contributor.authorPark, Byoung Chulen
dc.contributor.authorPark, Sung Gooen
dc.contributor.authorYi, Gwan-Suen
dc.contributor.authorChi, Seung-Wooken
dc.date.accessioned2018-11-23T04:39:06Zen
dc.date.accessioned2019-12-06T16:35:21Z-
dc.date.available2018-11-23T04:39:06Zen
dc.date.available2019-12-06T16:35:21Z-
dc.date.issued2014en
dc.identifier.citationLee, D.-H., Ha, J.-H., Kim, Y., Jang, M., Park, S. J., Yoon, H. S., . . . Chi, S.-W. (2014). A Conserved Mechanism for Binding of p53 DNA-Binding Domain and Anti-Apoptotic Bcl-2 Family Proteins. Molecules and Cells, 37(3), 264-269. doi:10.14348/molcells.2014.0001en
dc.identifier.issn1016-8478en
dc.identifier.urihttps://hdl.handle.net/10356/87108-
dc.identifier.urihttp://hdl.handle.net/10220/46692en
dc.description.abstractThe molecular interaction between tumor suppressor p53 and the anti-apoptotic Bcl-2 family proteins plays an essential role in the transcription-independent apoptotic pathway of p53. In this study, we investigated the binding of p53 DNA-binding domain (p53DBD) with the anti-apoptotic Bcl-2 family proteins, Bcl-w, Mcl-1, and Bcl-2, using GST pull-down assay and NMR spectroscopy. The GST pull-down assays and NMR experiments demonstrated the direct binding of the p53DBD with Bcl-w, Mcl-1, and Bcl-2. Further, NMR chemical shift perturbation data showed that Bcl-w and Mcl-1 bind to the positively charged DNA-binding surface of p53DBD. Noticeably, the refined structural models of the complexes between p53DBD and Bcl-w, Mcl-1, and Bcl-2 showed that the binding mode of p53DBD is highly conserved among the anti-apoptotic Bcl-2 family proteins. Furthermore, the chemical shift perturbations on Bcl-w, Mcl-1, and Bcl-2 induced by p53DBD binding occurred not only at the p53DBD-binding acidic region but also at the BH3 peptide-binding pocket, which suggests an allosteric conformational change similar to that observed in Bcl-XL. Taken altogether, our results revealed a structural basis for a conserved binding mechanism between p53DBD and the anti-apoptotic Bcl-2 family proteins, which shed light on to the molecular understanding of the transcription-independent apoptosis pathway of p53.en
dc.format.extent6 p.en
dc.language.isoenen
dc.relation.ispartofseriesMolecules and Cellsen
dc.rights© 2014 The Korean Society for Molecular and Cellular Biology. This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported License. To view a copy of this license, visit (http://creativecommons.org/licenses/by-nc-sa/3.0/).en
dc.subjectDRNTU::Science::Biological sciencesen
dc.subjectApoptosisen
dc.subjectBcl-2 Family Proteinsen
dc.titleA conserved mechanism for binding of p53 DNA-Binding domain and Anti-Apoptotic Bcl-2 family proteinsen
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen
dc.identifier.doihttp://dx.doi.org/10.14348/molcells.2014.0001en
dc.description.versionPublished versionen
item.grantfulltextopen-
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